Cofactor-Apoprotein Hydrogen Bonding in Oxidized and Fully Reduced Flavodoxin Monitored by Trans-Hydrogen-Bond Scalar Couplings

Hydrogen bonding plays a key role in the tight binding of the FMN cofactor and the regulation of its redox properties in flavodoxins. Hydrogen bonding interactions can be directly observed in solution by multidimensional heteronuclear NMR spectroscopy through the scalar couplings between donor and a...

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Published inChembiochem : a European journal of chemical biology Vol. 5; no. 11; pp. 1523 - 1534
Main Authors Löhr, Frank, Yalloway, Gary N, Mayhew, Stephen G, Rüterjans, Heinz
Format Journal Article
LanguageEnglish
Published Weinheim Wiley-VCH Verlag 05.11.2004
WILEY-VCH Verlag
WILEY‐VCH Verlag
Subjects
Apoproteins - chemistry
Apoproteins - metabolism
Desulfovibrio vulgaris
Desulfovibrio vulgaris - metabolism
flavin
Flavodoxin - chemistry
Flavodoxin - metabolism
Hydrogen Bonding
Models, Molecular
Molecular Structure
NMR spectroscopy
Nuclear Magnetic Resonance, Biomolecular - methods
Oxidation-Reduction
Protein Binding
protein structures
quantitative J correlation
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Structure-Activity Relationship
TROSY
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Abstract Hydrogen bonding plays a key role in the tight binding of the FMN cofactor and the regulation of its redox properties in flavodoxins. Hydrogen bonding interactions can be directly observed in solution by multidimensional heteronuclear NMR spectroscopy through the scalar couplings between donor and acceptor nuclei. Here we report on the detection of intermolecular trans-hydrogen-bond couplings (hJ) between the flavin ring system and the backbone of Desulfovibrio vulgaris flavodoxin in the oxidized and the two-electron reduced states. For this purpose, experiments are adapted from pulse sequences previously applied to determining hJ coupling constants in nucleic acid-base pairs and proteins. The resulting h²JN,N, h⁴JN,N, h³JC,N, and h¹JH,N couplings involve the ¹⁵N(1), ¹³C(2), and ¹⁵N(3) nuclei of the pyrimidine moiety of FMN, whereas no such interactions are detectable for ¹³C(4) and ¹⁵N(5). Several long-range ¹⁵N-¹⁵N, ¹³C-¹⁵N, and ¹H-¹⁵N J-coupling constants within the flavin are obtained as “by-products”. The magnitudes of both hJ and regular J couplings are found to be dependent on the redox state. In general, good correlations between hJ coupling constants and donor-group ¹H chemical shifts and also crystallographic donor-acceptor distances are observed.
AbstractList Hydrogen bonding plays a key role in the tight binding of the FMN cofactor and the regulation of its redox properties in flavodoxins. Hydrogen bonding interactions can be directly observed in solution by multidimensional heteronuclear NMR spectroscopy through the scalar couplings between donor and acceptor nuclei. Here we report on the detection of intermolecular trans-hydrogen-bond couplings ((h)J) between the flavin ring system and the backbone of Desulfovibrio vulgaris flavodoxin in the oxidized and the two-electron reduced states. For this purpose, experiments are adapted from pulse sequences previously applied to determining (h)J coupling constants in nucleic acid-base pairs and proteins. The resulting (h2)J(N,N), (h4)J(N,N), (h3)J(C,N), and (h1)J(H,N) couplings involve the (15)N(1), (13)C(2), and (15)N(3) nuclei of the pyrimidine moiety of FMN, whereas no such interactions are detectable for (13)C(4) and (15)N(5). Several long-range (15)N-(15)N, (13)C-(15)N, and (1)H-(15)N J-coupling constants within the flavin are obtained as "by-products". The magnitudes of both (h)J and regular J couplings are found to be dependent on the redox state. In general, good correlations between (h)J coupling constants and donor-group (1)H chemical shifts and also crystallographic donor-acceptor distances are observed.
Hydrogen bonding plays a key role in the tight binding of the FMN cofactor and the regulation of its redox properties in flavodoxins. Hydrogen bonding interactions can be directly observed in solution by multidimensional heteronuclear NMR spectroscopy through the scalar couplings between donor and acceptor nuclei. Here we report on the detection of intermolecular trans‐hydrogen‐bond couplings (hJ) between the flavin ring system and the backbone of Desulfovibrio vulgaris flavodoxin in the oxidized and the two‐electron reduced states. For this purpose, experiments are adapted from pulse sequences previously applied to determining hJ coupling constants in nucleic acid–base pairs and proteins. The resulting h2JN,N, h4JN,N, h3JC,N, and h1JH,N couplings involve the 15N(1), 13C(2), and 15N(3) nuclei of the pyrimidine moiety of FMN, whereas no such interactions are detectable for 13C(4) and 15N(5). Several long‐range 15N–15N, 13C–15N, and 1H–15N J‐coupling constants within the flavin are obtained as “by‐products”. The magnitudes of both hJ and regular J couplings are found to be dependent on the redox state. In general, good correlations between hJ coupling constants and donor‐group 1H chemical shifts and also crystallographic donor–acceptor distances are observed. HJ couplings make hydrogen bonds visible: unlike other NMR parameters they allow direct identification of both donor and acceptor groups. Hydrogen bonding is assumed to be important for the modulation of the cofactor's redox potentials in flavoproteins. This study describes the measurement of hJN,N and hJC,N couplings in the low‐potential electron‐carrier protein flavodoxin and compares their magnitudes in two redox states (see scheme).
Hydrogen bonding plays a key role in the tight binding of the FMN cofactor and the regulation of its redox properties in flavodoxins. Hydrogen bonding interactions can be directly observed in solution by multidimensional heteronuclear NMR spectroscopy through the scalar couplings between donor and acceptor nuclei. Here we report on the detection of intermolecular trans- hydrogen-bond couplings ( super(h)J) between the flavin ring system and the backbone of Desulfovibrio vulgaris flavodoxin in the oxidized and the two-electron reduced states. For this purpose, experiments are adapted from pulse sequences previously applied to determining super(h)J coupling constants in nucleic acid-base pairs and proteins. The resulting super(h2)J sub(N,N), super(h4)J sub(N,N), super(h3)J sub(C,N), and super(h1)J sub(H,N) couplings involve the super(15)N(1), super(13)C(2), and super(15)N(3) nuclei of the pyrimidine moiety of FMN, whereas no such interactions are detectable for super(13)C(4) and super(15)N(5). Several long-range super(15)N- super(15)N, super(13)C- super(15)N, and super(1)H- super(15)N J-coupling constants within the flavin are obtained as "by-products". The magnitudes of both super(h)J and regular J couplings are found to be dependent on the redox state. In general, good correlations between super(h)J coupling constants and donor-group super(1)H chemical shifts and also crystallographic donor-acceptor distances are observed.
Abstract Hydrogen bonding plays a key role in the tight binding of the FMN cofactor and the regulation of its redox properties in flavodoxins. Hydrogen bonding interactions can be directly observed in solution by multidimensional heteronuclear NMR spectroscopy through the scalar couplings between donor and acceptor nuclei. Here we report on the detection of intermolecular trans‐hydrogen‐bond couplings ( h J ) between the flavin ring system and the backbone of Desulfovibrio vulgaris flavodoxin in the oxidized and the two‐electron reduced states. For this purpose, experiments are adapted from pulse sequences previously applied to determining h J coupling constants in nucleic acid–base pairs and proteins. The resulting h2 J N,N , h4 J N,N , h3 J C,N , and h1 J H,N couplings involve the 15 N(1), 13 C(2), and 15 N(3) nuclei of the pyrimidine moiety of FMN, whereas no such interactions are detectable for 13 C(4) and 15 N(5). Several long‐range 15 N– 15 N, 13 C– 15 N, and 1 H– 15 N J ‐coupling constants within the flavin are obtained as “by‐products”. The magnitudes of both h J and regular J couplings are found to be dependent on the redox state. In general, good correlations between h J coupling constants and donor‐group 1 H chemical shifts and also crystallographic donor–acceptor distances are observed.
Hydrogen bonding plays a key role in the tight binding of the FMN cofactor and the regulation of its redox properties in flavodoxins. Hydrogen bonding interactions can be directly observed in solution by multidimensional heteronuclear NMR spectroscopy through the scalar couplings between donor and acceptor nuclei. Here we report on the detection of intermolecular trans-hydrogen-bond couplings (hJ) between the flavin ring system and the backbone of Desulfovibrio vulgaris flavodoxin in the oxidized and the two-electron reduced states. For this purpose, experiments are adapted from pulse sequences previously applied to determining hJ coupling constants in nucleic acid-base pairs and proteins. The resulting h²JN,N, h⁴JN,N, h³JC,N, and h¹JH,N couplings involve the ¹⁵N(1), ¹³C(2), and ¹⁵N(3) nuclei of the pyrimidine moiety of FMN, whereas no such interactions are detectable for ¹³C(4) and ¹⁵N(5). Several long-range ¹⁵N-¹⁵N, ¹³C-¹⁵N, and ¹H-¹⁵N J-coupling constants within the flavin are obtained as “by-products”. The magnitudes of both hJ and regular J couplings are found to be dependent on the redox state. In general, good correlations between hJ coupling constants and donor-group ¹H chemical shifts and also crystallographic donor-acceptor distances are observed.
Author Rüterjans, Heinz
Löhr, Frank
Yalloway, Gary N.
Mayhew, Stephen G.
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Cites_doi 10.1046/j.1432-1327.1998.2580362.x
10.1006/jmra.1995.1179
10.1021/bi00611a027
10.1126/science.278.5340.1128
10.1093/nar/27.15.3104
10.1021/bi00170a023
10.1016/0022-2364(83)90259-7
10.1021/bi973193k
10.1021/ja00497a058
10.1006/jmbi.1999.3151
10.1038/nsb0696-522
10.1016/0022-2364(89)90154-6
10.1021/ja030246e
10.1002/pro.5560011103
10.1021/ja990340o
10.1021/ja970876e
10.1021/ja970573k
10.1021/bi010571j
10.1016/0022-2836(91)90214-Q
10.1021/ja994255s
10.1021/ja003781c
10.1023/A:1020919131801
10.1073/pnas.69.11.3189
10.1002/1099-0534(2001)13:2<103::AID-CMR1001>3.0.CO;2-M
10.1021/ja981513x
10.1007/BF00224568
10.1021/ja00356a056
10.1016/0022-2364(83)90241-X
10.1017/S0033583500004911
10.1006/jmre.1998.1406
10.1002/1521-3765(20000818)6:16<2925::AID-CHEM2925>3.0.CO;2-M
10.1111/j.1432-1033.1990.tb19444.x
10.1023/A:1008346517302
10.1107/S0907444902012234
10.1146/annurev.mi.38.100184.003003
10.1016/0022-2364(92)90289-J
10.1016/S0065-3233(08)60129-1
10.1002/(SICI)1097-0134(19990515)35:3<275::AID-PROT1>3.0.CO;2-V
10.1021/ja9917417
10.1023/A:1008388400601
10.1006/jmre.2000.2048
10.1021/bi962180o
10.1021/bi00255a011
10.1007/BF00200433
10.1023/A:1022233103990
10.1006/jmrb.1996.0082
10.1023/A:1008268930690
10.1002/pro.5560070210
10.1021/ja9908321
10.1021/ja994204v
10.1016/0022-2836(77)90031-6
10.1021/ja000005w
10.1016/S0021-9258(18)55469-7
10.1016/0006-291X(70)90816-8
10.1023/A:1018380509735
10.1021/ja00052a088
10.1006/jmre.2000.2157
10.1017/S0033583500005217
10.1006/jmre.2000.2122
10.1006/jmre.1999.1998
10.1021/ja038616m
10.1021/ja00079a052
10.1110/ps.28602
10.1111/j.1432-1033.1983.tb07848.x
10.1016/0022-2364(82)90279-7
10.1006/jmre.1999.1899
10.1006/jmra.1994.1066
10.1016/S0040-4039(01)86031-7
10.1073/pnas.70.12.3857
10.1016/0022-2364(89)90183-2
10.1007/BF00211777
10.1111/j.1432-1033.1991.tb16475.x
10.1023/A:1008367405025
10.1021/ja00037a042
10.1021/bi00245a008
10.1007/BF00178258
10.1111/j.1432-1033.1993.tb17746.x
10.1021/ja00308a042
10.1021/ja9630553
10.1007/BF02192814
10.1046/j.1432-1327.1999.00767.x
10.1023/A:1008340116418
10.1002/pro.5560061205
10.1023/A:1026737732576
10.1016/0022-2364(70)90067-3
10.1016/0006-291X(66)90527-4
10.1111/j.1432-1033.1984.tb07942.x
10.1006/jmre.1997.1187
10.1021/ja029286t
10.1016/0022-2836(91)90884-9
10.1021/ja00004a075
10.1021/bi00370a010
10.1073/pnas.94.23.12366
10.1021/ja00038a084
10.1021/ja001345k
10.1073/pnas.95.24.14147
10.1021/ja003080f
10.1006/jmre.2000.2221
10.1021/ja012674v
10.1016/S0021-9258(18)96528-2
10.1006/jmre.1996.7482
10.1006/abbi.1994.1445
10.1023/A:1008335502416
10.1021/ja011618r
10.1016/S1874-6047(08)60225-5
10.1016/S0022-2836(83)80277-0
10.1023/A:1011265430149
10.1016/0009-2614(90)87025-M
10.1021/ja983945d
10.1111/j.1432-1033.1985.tb09067.x
10.1021/ja982649y
10.1111/j.1432-1033.1996.0190u.x
10.1023/A:1022814324367
10.1111/j.1432-1033.1996.0423z.x
10.1021/ja9909024
10.1021/ar010097
10.1021/ja003724j
10.1006/jmre.1998.1483
10.1016/0022-2364(85)90122-2
10.1021/bi00493a014
10.1021/ja00106a046
10.1021/ja9902221
10.1023/A:1011250219293
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References A. J. Dingley, S. Grzesiek, J. Am. Chem. Soc. 1998, 120, 8293-8297.
A. J. Dingley, F. Cordier, S. Grzesiek, Concepts Magn. Reson. 2001, 13, 103-127
M. Knauf, F. Löhr, M. Blümel, S. G. Mayhew, H. Rüterjans, Eur. J. Biochem. 1996, 238, 423-434
W. W. Smith, K. A. Pattridge, M. L. Ludwig, G. A. Petsko, D. Tsernoglou, M. Tanaka, K. T. Yasunobu, J. Mol. Biol. 1983, 165, 737-755
M. Barfield, A. J. Dingley, J. Feigon, S. Grzesiek, J. Am. Chem. Soc. 2001, 123, 4014-4022.
N. Tjandra, A. Bax, J. Am. Chem. Soc. 1997, 119, 8076-8082
S. Grzesiek, F. Cordier, A. J. Dingley in Methods in Enzymology, Vol. 338 (Eds.: T. L. James, V. Dötsch, U. Schmitz), Academic Press, San Diego, 2001, pp. 111-133
A. Hvidt, S. O. Nielsen, Adv. Protein Chem. 1966, 21, 287-386
K. Pervushin, G. Wider, K. Wüthrich, J. Biomol. NMR 1998, 12, 345-348
J. Freigang, K. Diederichs, K. P. Schäfer, W. Welte, R. Paul, Protein Sci. 2002, 11, 253-261
W. Watt, A. Tulinsky, R. P. Swenson, K. D. Watenpaugh, J. Mol. Biol. 1991, 218, 195-208
F. Löhr, S. G. Mayhew, H. Rüterjans, J. Am. Chem. Soc. 2000, 122, 9289-9295.
I. Vakonakis, A. C. LiWang, J. Biomol. NMR 2004, 29, 65-72.
J. Czernek, R. Brüschweiler, J. Am. Chem. Soc. 2001, 123, 11 079-11 080
A. O. Cuello, C. M. McIntosh, V. M. Rotello, J. Am. Chem. Soc. 2000, 124, 3517-3521.
J. Vervoort, D. Heering, S. Peelen, W. van Berkel in Methods in Enzymology, Vol. 243 (Eds.: H. D. Peck, Jr., J. LeGall), Academic Press, New York, 1994, pp. 188-203.
R. Fiala, J. Czernek, V. Sklenář, J. Biomol. NMR 2000, 16, 291-302
D. J. States, R. A. Haberkorn, D. J. Ruben, J. Magn. Reson. 1982, 48, 286-292.
S. T. Rao, F. Shaffie, C. Yu, K. A. Satyshur, B. J. Stockman, J. L. Markley, M. Sundaralingam, Protein Sci. 1992, 1, 1413-1427
C. T. Sharkey, S. G. Mayhew, T. M. Higgins, M. A. Walsh in Flavins and Flavoproteins (Eds.: K. J. Stevenson, V. Massey, C. H. Williams, Jr.), University of Calgary Press, Calgary, 1996, pp. 445-448
A. C. LiWang, A. Bax, J. Magn. Reson. 1997, 127, 54-64.
F.-C. Chang, L. H. Bradley, R. P. Swenson, Biochim. Biophys. Acta 2001, 1504, 319-328.
M. Hennig, B. H. Geierstanger, J. Am. Chem. Soc. 1999, 121, 5123-5126.
F. Cordier, S. Grzesiek, J. Am. Chem. Soc. 1999, 121, 1601-1602.
R. Artali, G. Bombieri, F. Meneghetti, G. Gilardi, S. J. Sadeghi, D. Cavazzini, G. L. Rossi, Acta Cryst. Sect. D 2002, 58, 1787-1792.
F. Löhr, S. Pfeiffer, Y.-J. Lin, J. Hartleib, O. Klimmek, H. Rüterjans, J. Biomol. NMR 2000, 18, 337-346
X. Yan, X. Kong, Y. Xia, K. H. Sze, G. Zhu, J. Magn. Reson. 2000, 147, 357-360.
P. Permi, I. Kilpeläinen, A. Annila, J. Magn. Reson. 2000, 146, 255-259
C. D. Poulter, C. L. Livingston, Tetrahedron Lett. 1979, 9, 755-758
A. C. LiWang, A. Bax, J. Am. Chem. Soc. 1996, 118, 12 864-12 865
K. Pervushin, A. Ono, C. Fernández, T. Szyperski, M. Kainosho, K. Wüthrich, Proc. Natl. Acad. Sci. USA 1998, 95, 14 147-14 151.
P. A. O'Farrell, M. A. Walsh, A. A. McCarthy, T. M. Higgins, G. Voordouw, S. G. Mayhew, Biochemistry 1998, 37, 8405-8416.
K. Kawano, N. Ohishi, A. T. Suzuki, Y. Kyogoku, K. Yagi, Biochemistry 1978, 17, 3854-3859.
J. Boyd, N. Soffe, J. Magn. Reson. 1989, 85, 406-413
S. G. Mayhew, Eur. J. Biochem. 1999, 265, 698-702.
I. Vakonakis, M. Salazar, M. Kang, K. R. Dunbar, A. C. LiWang, J. Biomol. NMR 2003, 25
S. G. Mayhew, M. L. Ludwig in The Enzymes, Vol. 12 (Ed.: P. D. Boyer), Academic Press, New York, 1975, pp. 57-118
H. D. Franken, H. Rüterjans, F. Müller, Eur. J. Biochem. 1984, 138, 481-489
J. Vervoort, F. Müller, J. LeGall, H. Sedlmaier, Eur. J. Biochem. 1985, 151, 49-57
A. Romero, J. Caldeira, J. LeGall, I. Moura, J. J. G. Moura, M. J. Romao, Eur. J. Biochem. 1996, 239, 190-196
F. Cordier, M. Barfield, S. Grzesiek, J. Am. Chem. Soc. 2003, 125, 15 750-15 751.
K. D. Watenpaugh, L. C. Sieker, L. H. Jensen, Proc. Natl. Acad. Sci. USA 1973, 70, 3857-3860
M. Mishima, S. Hatanaka, S. Yokoyama, T. Ikegami, M. Wälchli, Y. Ito, M. Shirakawa, J. Am. Chem. Soc. 2000, 122, 5883-5884.
A. Bax, G. W. Vuister, S. Grzesiek, F. Delaglio, A. C. Wang, R. Tschudin, G. Zhu in Methods in Enzymology, Vol. 239 (Eds.: T. L. James, N. J. Oppenheimer), Academic Press, New York, 1994, pp. 79-105.
R. E. London, J. Magn. Reson. 1990, 86, 410-415.
S. W. Englander, N. R. Kallenbach, Q. Rev. Biophys. 1983, 16, 521-655.
P. M. Bowers, R. E. Klevit, Nat. Struct. Biol. 1996, 3, 522-531
D. S. Wishart, C. G. Bigam, J. Yao, F. Abildgaard, H. J. Dyson, E. Oldfield, J. L. Markley, B. D. Sykes, J. Biomol. NMR 1995, 6, 135-140.
K. Pervushin, R. Riek, G. Wider, K. Wüthrich, Proc. Natl. Acad. Sci. USA 1997, 94, 12 366-12 371.
A. Bagno, Chem. Eur. J. 2000, 6, 2925-2930
M. Barfield, J. Am. Chem. Soc. 2002, 124, 4158-4168
A. Liu, W. Hu, S. Qamar, A. Majumdar, J. Biomol. NMR 2000, 17, 55-61.
F. Löhr, H. Rüterjans, J. Magn. Reson. 2000, 146, 126-131
J. M. Odom, H. D. Peck, Jr., Ann. Rev. Microbiol. 1984, 38, 551-592.
B. Luy, U. Richter, E. S. DeJong, O. W. Sørensen, J. P. Marino, J. Biomol. NMR 2002, 24, 133-142.
C. P. M. van Mierlo, P. Lijnzaad, J. Vervoort, F. Müller, H. J. C. Berendsen, J. de Vlieg, Eur. J. Biochem. 1990, 194, 185-198
D. S. Wishart, B. D. Sykes, F. M. Richards, J. Mol. Biol. 1991, 222, 311-333
S. Peelen, J. Vervoort, Arch. Biochem. Biophys. 1994, 314, 291-300.
P. R. Blake, J. B. Park, M. W. W. Adams, M. F. Summers, J. Am. Chem. Soc. 1992, 114, 4931-4933
A. Meissner, O. Sørensen, J. Magn. Reson. 2000, 143, 431-434.
G. Cornilescu, B. E. Ramirez, M. K. Frank, G. M. Clore, A. M. Gronenborn, A. Bax, J. Am. Chem. Soc. 1999, 121, 6275-6279.
T. Tuttle, E. Kraka, A. Wu, D. Cremer, J. Am. Chem. Soc. 2004, 126, 5093-5107.
S. Peelen, S. S. Wijmenga, P. J. A. Erbel, R. L. Robson, R. R. Eady, J. Vervoort, J. Biomol. NMR 1996, 7, 315-330
G. A. Morris, R. Freeman, J. Am. Chem. Soc. 1979, 101, 760-762.
K. Pervushin, C. Fernández, R. Riek, A. Ono, M. Kainosho, K. Wüthrich, J. Biomol. NMR 2000, 16, 39-46.
A. Eletsky, A. Kienhofer, K. Pervushin, J. Biomol. NMR 2001, 20, 177-180.
E. Knight, Jr., R. W. F. Hardy, J. Biol. Chem. 1966, 241, 2752-2756.
G. Wagner, Q. Rev. Biophys. 1983, 16, 1-57
H. L. J. Wienk, M. M. Martínez, G. N. Yalloway, J. M. Schmidt, C. Pérez, H. Rüterjans, F. Löhr, J. Biomol. NMR 2003, 25, 133-145.
C. Scheurer, R. Brüschweiler, J. Am. Chem. Soc. 1999, 121, 8661-8662
J. Weigelt, J. Am. Chem. Soc. 1998, 120, 10 778-10 779.
G. N. Yalloway, F. Löhr, H. Rüterjans, S. G. Mayhew in Flavins and Flavoproteins (Eds.: S. Chapman, R. Perham, N. Scrutton), Rudolf Weber Agency for Scientific Publications, Berlin, 2002, pp. 679-684.
L. Paolillo, E. D. Becker, J. Magn. Reson. 1970, 2, 168-173
L. Emsley, G. Bodenhausen, Chem. Phys. Lett. 1990, 165, 469-476.
M. Czisch, R. Boelens, J. Magn. Reson. 1998, 134, 158-160
M. L. Ludwig, C. L. Luschinsky in Chemistry and Biochemistry of Flavoenzymes, Vol. 3 (Ed.: F. Müller), CRC Press, Boca Raton, 1992, pp. 427-466
M. L. Ludwig, K. A. Pattridge, A. L. Metzger, M. M. Dixon, M. Eren, Y. Feng, R. P. Swenson, Biochemistry 1997, 36, 1259-1280
A. Hrovat, M. Blümel, F. Löhr, S. G. Mayhew, H. Rüterjans, J. Biomol. NMR 1997, 10, 53-62.
R. P. Simondsen, G. Tollin, Mol. Cell. Biochem. 1980, 33, 13-24
105-112.
F. Löhr, C. Pérez, J. M. Schmidt, H. Rüterjans, Bull. Magn. Reson. 1999, 20, 9-14
R. D. Andersen, P. A. Apgar, R. M. Burnett, G. D. Darling, M. E. LeQuesne, S. G. Mayhew, M. L. Ludwig, Proc. Natl. Acad. Sci. USA 1972, 69, 3189-3191
F. Cordier, M. Rogowski, S. Grzesiek, A. Bax, J. Magn. Reson. 1999, 140, 510-512.
G. N. Yalloway, F. Löhr, H. L. J. Wienk, S. G. Mayhew, A. Hrovat, M. A. Knauf, H. Rüterjans, J. Biomol. NMR 2003, 25, 257-258.
M. R. Bendall, D. T. Pegg, D. M. Doddrell, J. Magn. Reson. 1983, 52, 81-117.
A. J. Shaka, P. B. Barker, R. Freeman, J. Magn. Reson. 1985, 64, 547-552.
A. Liu, A. Majumdar, F. Jiang, N. Chernichenko, W. Skripkin, D. J. Patel, J. Am. Chem. Soc. 2000, 122, 11 226-11 227.
S. G. Mayhew, G. Tollin, in Chemistry and Biochemistry of Flavoenzymes, Vol. 3 (Ed.: F. Müller), CRC Press, Boca Raton, 1992, pp. 389-426
A. Pardi, G. Wagner, K. Wüthrich, Eur. J. Biochem. 1983, 137, 445-454.
L. H. Bradley, R. P. Swenson, Biochemistry 2001, 40, 8686-8695.
C. Wang, X. Gao, R. A. Jones, J. Am. Chem. Soc. 1991, 113, 1448-1450
C. L. Drennan, K. A. Pattridge, C. H. Weber, A. L. Metzger, D. M. Hoover, M. L. Ludwig, J. Mol. Biol. 1999, 294, 711-724
A. Bax, R. H. Griffey, B. L. Hawkins, J. Magn. Reson. 1983, 55, 301-315
J. Wöhnert, A. J. Dingley, M. Stoldt, M. Görlach, S. Grzesiek, L. R. Brown, Nucleic Acids Res. 1999, 27, 3104-3110.
G. T. Montelione, M. E. Winkler, P. Rauenbuehler, G. Wagner, J. Magn. Reson. 1989, 82, 198-204.
A. Liu, A. Majumdar, W. Hu, A. Kettani, E. Skripkin, D. J. Patel, J. Am. Chem. Soc. 2000, 122, 3206-3210.
R. R. Shoup, H. T. Miles, E. D. Becker, Biochem. Biophys. Res. Commun. 1966, 23, 194-201
B. J. Stockman, A. M. Krezel, J. L. Markley, K. G. Leonhardt, N. A. Straus, Biochemistry 1990, 29, 9600-9609
F. Löhr, H. Rüterjans, J. Magn. Reson. 1998, 132, 130-137.
G. P. Curley, M. C. Carr, S. G. Mayhew, G. Voordouw, Eur. J. Biochem. 1991, 202, 1091-1100.
A. Dingley, F. Cordier, V. A. Jaravine, S. Grzesiek in Methods and Principles in Medicinal Chemistry, Vol. 16 (Ed.: O. Zerbe), Wiley-VCH, Weinheim, 2003, pp. 207-226.
P. R. Blake, B. Lee, M. F. Summers, M. W. W. Adams, J. B. Park, Z. H. Zhou, A. Bax, J. Biomol. NMR 1992, 2, 527-533.
E. Steensma, N. J. M. Nijman, Y. J. M. Bollen, P. A. de Jager, W. A. M. van den Berg, W. M. A. M. van Dongen, C. P. M. van Mierlo, Protein Sci. 1998, 7, 306-317.
S. Grzesiek, A. Bax, J. Am. Chem. Soc. 1993, 115, 12 593-12 594
N. Jurani , P. K. Ilich, S. Macura, J. Am. Chem. Soc. 1995, 117, 405-410
Chemistry and Biochemistry of Flavoenzymes, Vols. 1-3 (Ed.: F. Müller), CRC Press, Boca Raton, 1992.
M. Tessari, H. Vis, R. Boelens, R. Kaptein, G. W. Vuister, J. Am. Chem. Soc. 1997, 119, 8985-8990.
C. Griesinger, O. W. Sørensen, R. R. Ernst, J. Am. Chem. Soc. 1985, 107, 6394-6396
K. Fukuyama, S. Wakabayashi, H. Matsubara, L. J. Rogers, J. Biol. Chem. 1990, 265, 15 804-15 812
S. Patt, J. Magn. Reson. 1992, 96, 94-102.
B. J. Stockman, A. Euvrad, D. A. Kloosterman, T. A. Scahill, R.
1997; 278
1991; 113
2002; 11
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2004; 2
1997; 6
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2001; 40
2000; 18
1991; 222
2000; 16
2000; 17
2000; 124
1980; 33
1992; 114
1999; 294
2000; 122
1998; 95
1992; 1
1992; 2
1998; 12
1992; 3
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1983; 137
1994; 314
1999; 27
1992; 1–3
1996
1998; 258
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1972; 69
1998; 132
1998; 134
1995; 6
2001; 20
1991; 218
1982; 48
1991; 202
1984; 38
1990; 29
2002; 124
1997; 36
1986; 25
1999; 35
2003; 25
1996; 111
1977; 117
1998; 7
1985; 151
1993; 115
2003; 20
1996; 239
1996; 118
1990; 194
1996; 238
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2002; 58
1989; 82
2004; 126
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1999; 121
2003; 16
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1985; 64
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2001; 13
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1999; 265
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2000; 143
e_1_2_5_120_2
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e_1_2_5_46_2
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e_1_2_5_80_2
e_1_2_5_61_2
e_1_2_5_84_2
(e_1_2_5_1_2) 1992
Ludwig M. L. (e_1_2_5_6_2) 1992
e_1_2_5_38_2
e_1_2_5_155_2
e_1_2_5_15_2
e_1_2_5_57_2
London R. E. (e_1_2_5_123_2) 1990; 86
e_1_2_5_34_2
e_1_2_5_113_2
e_1_2_5_151_2
e_1_2_5_11_2
e_1_2_5_53_2
e_1_2_5_132_2
e_1_2_5_3_2
e_1_2_5_76_2
e_1_2_5_117_2
e_1_2_5_99_2
e_1_2_5_136_2
Löhr F. (e_1_2_5_107_2) 1999; 20
e_1_2_5_159_2
e_1_2_5_19_2
e_1_2_5_91_2
e_1_2_5_72_2
e_1_2_5_95_2
e_1_2_5_30_2
Vakonakis I. (e_1_2_5_48_2) 2004; 2
Mayhew S. G. (e_1_2_5_5_2) 1992
e_1_2_5_26_2
e_1_2_5_49_2
e_1_2_5_45_3
e_1_2_5_146_2
e_1_2_5_22_2
e_1_2_5_161_2
Chang F.‐C. (e_1_2_5_121_2) 2001
e_1_2_5_142_2
e_1_2_5_64_2
e_1_2_5_127_2
e_1_2_5_104_2
e_1_2_5_68_2
e_1_2_5_108_2
e_1_2_5_60_2
e_1_2_5_83_2
e_1_2_5_41_2
Yalloway G. N. (e_1_2_5_101_2) 2002
e_1_2_5_14_2
e_1_2_5_37_2
e_1_2_5_131_2
e_1_2_5_154_2
e_1_2_5_8_2
e_1_2_5_10_2
e_1_2_5_33_2
e_1_2_5_56_2
e_1_2_5_112_2
e_1_2_5_135_2
e_1_2_5_150_2
Vervoort J. (e_1_2_5_7_2) 1994
e_1_2_5_4_2
e_1_2_5_75_2
e_1_2_5_98_2
e_1_2_5_116_2
e_1_2_5_139_2
Bax A. (e_1_2_5_100_2) 1994
e_1_2_5_18_2
e_1_2_5_79_2
e_1_2_5_158_2
Sharkey C. T. (e_1_2_5_16_2) 1996
Dingley A. (e_1_2_5_88_2) 2003
e_1_2_5_90_2
e_1_2_5_71_2
e_1_2_5_94_2
e_1_2_5_52_2
e_1_2_5_145_2
e_1_2_5_25_2
e_1_2_5_44_2
e_1_2_5_122_2
e_1_2_5_141_2
e_1_2_5_21_2
e_1_2_5_103_2
e_1_2_5_126_2
e_1_2_5_67_2
e_1_2_5_149_2
e_1_2_5_29_2
Grzesiek S. (e_1_2_5_86_2) 2001
e_1_2_5_82_2
e_1_2_5_63_2
e_1_2_5_40_2
e_1_2_5_13_2
e_1_2_5_59_2
e_1_2_5_130_2
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e_1_2_5_111_2
e_1_2_5_153_2
e_1_2_5_97_2
e_1_2_5_138_2
Vakonakis I. (e_1_2_5_45_2) 2003; 2
e_1_2_5_78_2
e_1_2_5_115_2
e_1_2_5_17_2
e_1_2_5_119_2
e_1_2_5_70_2
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Grzesiek S. (e_1_2_5_87_2) 2003
e_1_2_5_62_2
e_1_2_5_85_2
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e_1_2_5_114_2
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e_1_2_5_50_2
References_xml – volume: 38
  start-page: 551
  year: 1984
  end-page: 592
  publication-title: Ann. Rev. Microbiol.
– volume: 20
  start-page: 9
  year: 1999
  end-page: 14
  publication-title: Bull. Magn. Reson.
– volume: 1
  start-page: 1413
  year: 1992
  end-page: 1427
  publication-title: Protein Sci.
– volume: 118
  start-page: 12 864
  year: 1996
  end-page: 12 865
  publication-title: J. Am. Chem. Soc.
– volume: 85
  start-page: 406
  year: 1989
  end-page: 413
  publication-title: J. Magn. Reson.
– volume: 124
  start-page: 4158
  year: 2002
  end-page: 4168
  publication-title: J. Am. Chem. Soc.
– volume: 101
  start-page: 760
  year: 1979
  end-page: 762
  publication-title: J. Am. Chem. Soc.
– volume: 37
  start-page: 8405
  year: 1998
  end-page: 8416
  publication-title: Biochemistry
– volume: 239
  start-page: 79
  year: 1994
  end-page: 105
– volume: 25
  start-page: 133
  year: 2003
  end-page: 145
  publication-title: J. Biomol. NMR
– volume: 123
  start-page: 7081
  year: 2001
  end-page: 7093
  publication-title: J. Am. Chem. Soc.
– volume: 2
  start-page: 527
  year: 1992
  end-page: 533
  publication-title: J. Biomol. NMR
– volume: 124
  start-page: 3517
  year: 2000
  end-page: 3521
  publication-title: J. Am. Chem. Soc.
– volume: 121
  start-page: 5123
  year: 1999
  end-page: 5126
  publication-title: J. Am. Chem. Soc.
– volume: 278
  start-page: 1128
  year: 1997
  end-page: 1132
  publication-title: Science
– volume: 33
  start-page: 15 298
  year: 1994
  end-page: 15 308
  publication-title: Biochemistry
– volume: 16
  start-page: 39
  year: 2000
  end-page: 46
  publication-title: J. Biomol. NMR
– volume: 114
  start-page: 4931
  year: 1992
  end-page: 4933
  publication-title: J. Am. Chem. Soc.
– volume: 119
  start-page: 8076
  year: 1997
  end-page: 8082
  publication-title: J. Am. Chem. Soc.
– volume: 202,
  start-page: 1091
  year: 1991
  end-page: 1100
  publication-title: Eur. J. Biochem.
– start-page: 679
  year: 2002
  end-page: 684
– volume: 111
  start-page: 194
  year: 1996
  end-page: 198
  publication-title: J. Magn. Reson. Ser. B
– volume: 95
  start-page: 14 147
  year: 1998
  end-page: 14 151
  publication-title: Proc. Natl. Acad. Sci. USA
– volume: 36
  start-page: 1259
  year: 1997
  end-page: 1280
  publication-title: Biochemistry
– volume: 123
  start-page: 4014
  year: 2001
  end-page: 4022
  publication-title: J. Am. Chem. Soc.
– volume: 16
  start-page: 1
  year: 1983
  end-page: 57
  publication-title: Q. Rev. Biophys.
– volume: 119
  start-page: 8985
  year: 1997
  end-page: 8990
  publication-title: J. Am. Chem. Soc.
– volume: 121
  start-page: 1601
  year: 1999
  end-page: 1602
  publication-title: J. Am. Chem. Soc.
– volume: 258
  start-page: 362
  year: 1998
  end-page: 371
  publication-title: Eur. J. Biochem.
– volume: 114
  start-page: 4320
  year: 1992
  end-page: 4326
  publication-title: J. Am. Chem. Soc.
– volume: 35
  start-page: 275
  year: 1999
  end-page: 282
  publication-title: Proteins: Struct. Funct. Genet.
– volume: 120
  start-page: 10 778
  year: 1998
  end-page: 10 779
  publication-title: J. Am. Chem. Soc.
– volume: 7
  start-page: 306
  year: 1998
  end-page: 317
  publication-title: Protein Sci.
– volume: 107
  start-page: 6394
  year: 1985
  end-page: 6396
  publication-title: J. Am. Chem. Soc.
– volume: 122
  start-page: 3206
  year: 2000
  end-page: 3210
  publication-title: J. Am. Chem. Soc.
– volume: 140
  start-page: 510
  year: 1999
  end-page: 512
  publication-title: J. Magn. Reson.
– volume: 33
  start-page: 1029
  year: 1994
  end-page: 1036
  publication-title: Biochemistry
– volume: 13
  start-page: 103
  year: 2001
  end-page: 127
  publication-title: Concepts Magn. Reson.
– volume: 2
  start-page: 5
  year: 2003
  publication-title: J. Biomol. NMR 105–112.
– volume: 165
  start-page: 469
  year: 1990
  end-page: 476
  publication-title: Chem. Phys. Lett.
– volume: 117
  start-page: 195
  year: 1977
  end-page: 225
  publication-title: J. Mol. Biol.
– volume: 11
  start-page: 253
  year: 2002
  end-page: 261
  publication-title: Protein Sci.
– volume: 132
  start-page: 130
  year: 1998
  end-page: 137
  publication-title: J. Magn. Reson.
– volume: 40
  start-page: 8686
  year: 2001
  end-page: 8695
  publication-title: Biochemistry
– volume: 6
  start-page: 2525
  year: 1997
  end-page: 2537
  publication-title: Protein Sci.
– volume: 10
  start-page: 53
  year: 1997
  end-page: 62
  publication-title: J. Biomol. NMR
– volume: 17
  start-page: 3854
  year: 1978
  end-page: 3859
  publication-title: Biochemistry
– start-page: 1504
  year: 2001
  end-page: 328
  publication-title: Biochim. Biophys. Acta
– volume: 121
  start-page: 6275
  year: 1999
  end-page: 6279
  publication-title: J. Am. Chem. Soc.
– volume: 21
  start-page: 287
  year: 1966
  end-page: 386
  publication-title: Adv. Protein Chem.
– volume: 52
  start-page: 81
  year: 1983
  end-page: 117
  publication-title: J. Magn. Reson.
– volume: 121
  start-page: 6019
  year: 1999
  end-page: 6027
  publication-title: J. Am. Chem. Soc.
– volume: 122
  start-page: 5883
  year: 2000
  end-page: 5884
  publication-title: J. Am. Chem. Soc.
– volume: 3
  start-page: 427
  year: 1992
  end-page: 466
– volume: 107
  start-page: 178
  year: 1994
  end-page: 184
  publication-title: J. Magn. Reson. Ser. A
– volume: 218
  start-page: 195
  year: 1991
  end-page: 208
  publication-title: J. Mol. Biol.
– volume: 121
  start-page: 8661
  year: 1999
  end-page: 8662
  publication-title: J. Am. Chem. Soc.
– volume: 64
  start-page: 547
  year: 1985
  end-page: 552
  publication-title: J. Magn. Reson.
– start-page: 445
  year: 1996
  end-page: 448
– volume: 124
  start-page: 61
  year: 1997
  end-page: 71
  publication-title: J. Magn. Reson.
– volume: 55
  start-page: 301
  year: 1983
  end-page: 315
  publication-title: J. Magn. Reson.
– volume: 94
  start-page: 12 366
  year: 1997
  end-page: 12 371
  publication-title: Proc. Natl. Acad. Sci. USA
– volume: 25
  start-page: 257
  year: 2003
  end-page: 258
  publication-title: J. Biomol. NMR
– volume: 14
  start-page: 181
  year: 1999
  end-page: 184
  publication-title: J. Biomol. NMR
– volume: 1–3
  year: 1992
– volume: 134
  start-page: 158
  year: 1998
  end-page: 160
  publication-title: J. Magn. Reson.
– volume: 239
  start-page: 190
  year: 1996
  end-page: 196
  publication-title: Eur. J. Biochem.
– volume: 151
  start-page: 49
  year: 1985
  end-page: 57
  publication-title: Eur. J. Biochem.
– volume: 48
  start-page: 286
  year: 1982
  end-page: 292
  publication-title: J. Magn. Reson.
– volume: 265,
  start-page: 698
  year: 1999
  end-page: 702
  publication-title: Eur. J. Biochem.
– volume: 194
  start-page: 185
  year: 1990
  end-page: 198
  publication-title: Eur. J. Biochem.
– volume: 265
  start-page: 15 804
  year: 1990
  end-page: 15 812
  publication-title: J. Biol. Chem.
– volume: 115
  start-page: 273
  year: 1995
  end-page: 276
  publication-title: J. Magn. Reson. Ser. A
– volume: 82
  start-page: 198
  year: 1989
  end-page: 204
  publication-title: J. Magn. Reson.
– volume: 14
  start-page: 67
  year: 1999
  end-page: 70
  publication-title: J. Biomol. NMR
– volume: 115
  start-page: 12 593
  year: 1993
  end-page: 12 594
  publication-title: J. Am. Chem. Soc.
– volume: 7,
  start-page: 315
  year: 1996
  end-page: 330
  publication-title: J. Biomol. NMR
– volume: 2
  start-page: 9
  year: 2004
  end-page: 72
  publication-title: J. Biomol. NMR
– volume: 35
  start-page: 1
  year: 2002
  end-page: 11
  publication-title: Acc. Chem. Res.
– volume: 120
  start-page: 8293
  year: 1998
  publication-title: J. Am. Chem. Soc.
– volume: 33
  start-page: 13
  year: 1980
  end-page: 24
  publication-title: Mol. Cell. Biochem.
– volume: 146
  start-page: 126
  year: 2000
  end-page: 131
  publication-title: J. Magn. Reson.
– volume: 3
  start-page: 389
  year: 1992
  end-page: 426
– volume: 165
  start-page: 737
  year: 1983
  end-page: 755
  publication-title: J. Mol. Biol.
– volume: 24
  start-page: 133
  year: 2002
  end-page: 142
  publication-title: J. Biomol. NMR
– volume: 3
  start-page: 522
  year: 1996
  end-page: 531
  publication-title: Nat. Struct. Biol.
– volume: 222
  start-page: 311
  year: 1991
  end-page: 333
  publication-title: J. Mol. Biol.
– volume: 243
  start-page: 188
  year: 1994
  end-page: 203
– volume: 146
  start-page: 255
  year: 2000
  end-page: 259
  publication-title: J. Magn. Reson.
– volume: 126
  start-page: 5093
  year: 2004
  end-page: 5107
  publication-title: J. Am. Chem. Soc.
– volume: 3
  start-page: 133
  year: 1993
  end-page: 149
  publication-title: J. Biomol. NMR
– volume: 27
  start-page: 3104
  year: 1999
  end-page: 3110
  publication-title: Nucleic Acids Res.
– volume: 25
  start-page: 6789
  year: 1986
  end-page: 6799
  publication-title: Biochemistry
– volume: 241
  start-page: 2752
  year: 1966
  end-page: 2756
  publication-title: J. Biol. Chem.
– volume: 38
  start-page: 965
  year: 1970
  end-page: 972
  publication-title: Biochem. Biophys. Res. Commun.
– volume: 137
  start-page: 445
  year: 1983
  end-page: 454
  publication-title: Eur. J. Biochem.
– volume: 16
  start-page: 521
  year: 1983
  end-page: 655
  publication-title: Q. Rev. Biophys.
– volume: 105
  start-page: 5948
  year: 1983
  end-page: 5949
  publication-title: J. Am. Chem. Soc.
– volume: 58
  start-page: 1787
  year: 2002
  end-page: 1792
  publication-title: Acta Cryst. Sect. D
– volume: 121
  start-page: 2949
  year: 1999
  end-page: 2950
  publication-title: J. Am. Chem. Soc.
– volume: 125
  start-page: 15 750
  year: 2003
  end-page: 15 751
  publication-title: J. Am. Chem. Soc.
– volume: 16
  start-page: 291
  year: 2000
  end-page: 302
  publication-title: J. Biomol. NMR
– volume: 69
  start-page: 3189
  year: 1972
  end-page: 3191
  publication-title: Proc. Natl. Acad. Sci. USA
– volume: 2
  start-page: 168
  year: 1970
  end-page: 173
  publication-title: J. Magn. Reson.
– volume: 122
  start-page: 11 226
  year: 2000
  end-page: 11 227
  publication-title: J. Am. Chem. Soc.
– volume: 29
  start-page: 9600
  year: 1990
  end-page: 9609
  publication-title: Biochemistry
– volume: 86
  start-page: 410
  year: 1990
  end-page: 415
  publication-title: J. Magn. Reson.
– volume: 70
  start-page: 3857
  year: 1973
  end-page: 3860
  publication-title: Proc. Natl. Acad. Sci. USA
– volume: 125
  start-page: 4676
  year: 2003
  end-page: 4677
  publication-title: J. Am. Chem. Soc.
– volume: 23
  start-page: 194
  year: 1966
  end-page: 201
  publication-title: Biochem. Biophys. Res. Commun.
– volume: 12
  start-page: 57
  year: 1975
  end-page: 118
– volume: 127
  start-page: 54
  year: 1997
  end-page: 64
  publication-title: J. Magn. Reson.
– volume: 314
  start-page: 291
  year: 1994
  end-page: 300
  publication-title: Arch. Biochem. Biophys.
– volume: 6
  start-page: 135
  year: 1995
  end-page: 140
  publication-title: J. Biomol. NMR
– volume: 113
  start-page: 1448
  year: 1991
  end-page: 1450
  publication-title: J. Am. Chem. Soc.
– volume: 12
  start-page: 345
  year: 1998
  end-page: 348
  publication-title: J. Biomol. NMR
– volume: 238
  start-page: 423
  year: 1996
  end-page: 434
  publication-title: Eur. J. Biochem.
– volume: 16
  start-page: 207
  year: 2003
  end-page: 226
– volume: 19
  start-page: 361
  year: 2001
  end-page: 365
  publication-title: J. Biomol. NMR
– volume: 20
  start-page: 177
  year: 2001
  end-page: 180
  publication-title: J. Biomol. NMR
– volume: 338
  start-page: 111
  year: 2001
  end-page: 133
– volume: 123
  start-page: 11 079
  year: 2001
  end-page: 11 080
  publication-title: J. Am. Chem. Soc.
– volume: 9
  start-page: 755
  year: 1979
  end-page: 758
  publication-title: Tetrahedron Lett.
– volume: 30
  start-page: 7718
  year: 1991
  end-page: 7730
  publication-title: Biochemistry
– volume: 18
  start-page: 337
  year: 2000
  end-page: 346
  publication-title: J. Biomol. NMR
– volume: 114
  start-page: 10 663
  year: 1992
  end-page: 10 665
  publication-title: J. Am. Chem. Soc.
– volume: 117
  start-page: 405
  year: 1995
  end-page: 410
  publication-title: J. Am. Chem. Soc.
– volume: 147
  start-page: 357
  year: 2000
  end-page: 360
  publication-title: J. Magn. Reson.
– volume: 96
  start-page: 94
  year: 1992
  end-page: 102
  publication-title: J. Magn. Reson.
– volume: 213
  start-page: 167
  year: 1993
  end-page: 184
  publication-title: Eur. J. Biochem.
– volume: 138
  start-page: 481
  year: 1984
  end-page: 489
  publication-title: Eur. J. Biochem.
– volume: 143
  start-page: 387
  year: 2000
  end-page: 390
  publication-title: J. Magn. Reson.
– volume: 6
  start-page: 2925
  year: 2000
  end-page: 2930
  publication-title: Chem. Eur. J.
– volume: 122
  start-page: 9289
  year: 2000
  end-page: 9295
  publication-title: J. Am. Chem. Soc.
– volume: 17
  start-page: 55
  year: 2000
  end-page: 61
  publication-title: J. Biomol. NMR
– volume: 143
  start-page: 431
  year: 2000
  end-page: 434
  publication-title: J. Magn. Reson.
– volume: 20
  start-page: 255
  year: 2003
  end-page: 283
– volume: 294
  start-page: 711
  year: 1999
  end-page: 724
  publication-title: J. Mol. Biol.
– ident: e_1_2_5_110_2
– ident: e_1_2_5_155_2
– ident: e_1_2_5_2_2
– ident: e_1_2_5_20_2
  doi: 10.1046/j.1432-1327.1998.2580362.x
– volume: 20
  start-page: 9
  year: 1999
  ident: e_1_2_5_107_2
  publication-title: Bull. Magn. Reson.
  contributor:
    fullname: Löhr F.
– ident: e_1_2_5_154_2
  doi: 10.1006/jmra.1995.1179
– ident: e_1_2_5_120_2
  doi: 10.1021/bi00611a027
– ident: e_1_2_5_141_2
– ident: e_1_2_5_64_2
  doi: 10.1126/science.278.5340.1128
– ident: e_1_2_5_143_2
  doi: 10.1093/nar/27.15.3104
– ident: e_1_2_5_41_2
  doi: 10.1021/bi00170a023
– start-page: 188
  volume-title: Methods in Enzymology
  year: 1994
  ident: e_1_2_5_7_2
  contributor:
    fullname: Vervoort J.
– ident: e_1_2_5_119_2
  doi: 10.1016/0022-2364(83)90259-7
– ident: e_1_2_5_142_2
  doi: 10.1021/bi973193k
– ident: e_1_2_5_45_3
– ident: e_1_2_5_116_2
  doi: 10.1021/ja00497a058
– ident: e_1_2_5_21_2
  doi: 10.1006/jmbi.1999.3151
– ident: e_1_2_5_24_2
– ident: e_1_2_5_43_2
  doi: 10.1038/nsb0696-522
– ident: e_1_2_5_69_2
– ident: e_1_2_5_40_2
– ident: e_1_2_5_162_2
  doi: 10.1016/0022-2364(89)90154-6
– ident: e_1_2_5_99_2
– ident: e_1_2_5_54_2
– ident: e_1_2_5_140_2
  doi: 10.1021/ja030246e
– ident: e_1_2_5_15_2
  doi: 10.1002/pro.5560011103
– ident: e_1_2_5_144_2
  doi: 10.1021/ja990340o
– ident: e_1_2_5_55_2
  doi: 10.1021/ja970876e
– ident: e_1_2_5_56_2
  doi: 10.1021/ja970573k
– ident: e_1_2_5_106_2
– ident: e_1_2_5_146_2
  doi: 10.1021/bi010571j
– ident: e_1_2_5_52_2
  doi: 10.1016/0022-2836(91)90214-Q
– ident: e_1_2_5_78_2
  doi: 10.1021/ja994255s
– ident: e_1_2_5_130_2
  doi: 10.1021/ja003781c
– ident: e_1_2_5_82_2
  doi: 10.1023/A:1020919131801
– start-page: 79
  volume-title: Methods in Enzymology
  year: 1994
  ident: e_1_2_5_100_2
  contributor:
    fullname: Bax A.
– ident: e_1_2_5_9_2
  doi: 10.1073/pnas.69.11.3189
– ident: e_1_2_5_85_2
  doi: 10.1002/1099-0534(2001)13:2<103::AID-CMR1001>3.0.CO;2-M
– ident: e_1_2_5_72_2
  doi: 10.1021/ja981513x
– ident: e_1_2_5_4_2
  doi: 10.1007/BF00224568
– ident: e_1_2_5_51_2
  doi: 10.1021/ja00356a056
– ident: e_1_2_5_118_2
  doi: 10.1016/0022-2364(83)90241-X
– volume: 86
  start-page: 410
  year: 1990
  ident: e_1_2_5_123_2
  publication-title: J. Magn. Reson.
  contributor:
    fullname: London R. E.
– ident: e_1_2_5_38_2
  doi: 10.1017/S0033583500004911
– ident: e_1_2_5_102_2
  doi: 10.1006/jmre.1998.1406
– ident: e_1_2_5_36_2
– ident: e_1_2_5_137_2
  doi: 10.1002/1521-3765(20000818)6:16<2925::AID-CHEM2925>3.0.CO;2-M
– ident: e_1_2_5_25_2
  doi: 10.1111/j.1432-1033.1990.tb19444.x
– ident: e_1_2_5_135_2
– ident: e_1_2_5_105_2
  doi: 10.1023/A:1008346517302
– ident: e_1_2_5_23_2
  doi: 10.1107/S0907444902012234
– ident: e_1_2_5_35_2
  doi: 10.1146/annurev.mi.38.100184.003003
– ident: e_1_2_5_163_2
  doi: 10.1016/0022-2364(92)90289-J
– ident: e_1_2_5_37_2
  doi: 10.1016/S0065-3233(08)60129-1
– ident: e_1_2_5_44_2
  doi: 10.1002/(SICI)1097-0134(19990515)35:3<275::AID-PROT1>3.0.CO;2-V
– ident: e_1_2_5_49_2
– ident: e_1_2_5_136_2
  doi: 10.1021/ja9917417
– ident: e_1_2_5_156_2
  doi: 10.1023/A:1008388400601
– ident: e_1_2_5_81_2
  doi: 10.1006/jmre.2000.2048
– start-page: 207
  volume-title: Methods and Principles in Medicinal Chemistry
  year: 2003
  ident: e_1_2_5_88_2
  contributor:
    fullname: Dingley A.
– start-page: 679
  volume-title: Flavins and Flavoproteins
  year: 2002
  ident: e_1_2_5_101_2
  contributor:
    fullname: Yalloway G. N.
– ident: e_1_2_5_19_2
  doi: 10.1021/bi962180o
– ident: e_1_2_5_28_2
  doi: 10.1021/bi00255a011
– ident: e_1_2_5_65_2
– ident: e_1_2_5_148_2
– ident: e_1_2_5_30_2
  doi: 10.1007/BF00200433
– start-page: 445
  volume-title: Flavins and Flavoproteins
  year: 1996
  ident: e_1_2_5_16_2
  contributor:
    fullname: Sharkey C. T.
– ident: e_1_2_5_93_2
– ident: e_1_2_5_109_2
  doi: 10.1023/A:1022233103990
– ident: e_1_2_5_113_2
  doi: 10.1006/jmrb.1996.0082
– ident: e_1_2_5_151_2
  doi: 10.1023/A:1008268930690
– ident: e_1_2_5_84_2
– ident: e_1_2_5_31_2
  doi: 10.1002/pro.5560070210
– ident: e_1_2_5_76_2
  doi: 10.1021/ja9908321
– ident: e_1_2_5_145_2
  doi: 10.1021/ja994204v
– ident: e_1_2_5_11_2
  doi: 10.1016/0022-2836(77)90031-6
– ident: e_1_2_5_90_2
  doi: 10.1021/ja000005w
– ident: e_1_2_5_161_2
– ident: e_1_2_5_13_2
  doi: 10.1016/S0021-9258(18)55469-7
– ident: e_1_2_5_34_2
  doi: 10.1016/0006-291X(70)90816-8
– ident: e_1_2_5_126_2
  doi: 10.1023/A:1018380509735
– ident: e_1_2_5_149_2
  doi: 10.1021/ja00052a088
– ident: e_1_2_5_157_2
  doi: 10.1006/jmre.2000.2157
– ident: e_1_2_5_39_2
  doi: 10.1017/S0033583500005217
– ident: e_1_2_5_108_2
  doi: 10.1006/jmre.2000.2122
– ident: e_1_2_5_80_2
  doi: 10.1006/jmre.1999.1998
– ident: e_1_2_5_83_2
  doi: 10.1021/ja038616m
– ident: e_1_2_5_111_2
  doi: 10.1021/ja00079a052
– ident: e_1_2_5_33_2
– start-page: 111
  volume-title: Methods in Enzymology
  year: 2001
  ident: e_1_2_5_86_2
  contributor:
    fullname: Grzesiek S.
– volume: 2
  start-page: 5
  year: 2003
  ident: e_1_2_5_45_2
  publication-title: J. Biomol. NMR
  contributor:
    fullname: Vakonakis I.
– ident: e_1_2_5_22_2
  doi: 10.1110/ps.28602
– volume-title: Chemistry and Biochemistry of Flavoenzymes
  year: 1992
  ident: e_1_2_5_1_2
– start-page: 255
  volume-title: Biological Magnetic Resonance
  year: 2003
  ident: e_1_2_5_87_2
  contributor:
    fullname: Grzesiek S.
– ident: e_1_2_5_8_2
– ident: e_1_2_5_134_2
  doi: 10.1111/j.1432-1033.1983.tb07848.x
– ident: e_1_2_5_115_2
  doi: 10.1016/0022-2364(82)90279-7
– ident: e_1_2_5_79_2
  doi: 10.1006/jmre.1999.1899
– ident: e_1_2_5_112_2
  doi: 10.1006/jmra.1994.1066
– ident: e_1_2_5_62_2
  doi: 10.1016/S0040-4039(01)86031-7
– ident: e_1_2_5_10_2
  doi: 10.1073/pnas.70.12.3857
– ident: e_1_2_5_46_2
– ident: e_1_2_5_129_2
  doi: 10.1016/0022-2364(89)90183-2
– ident: e_1_2_5_153_2
  doi: 10.1007/BF00211777
– ident: e_1_2_5_98_2
  doi: 10.1111/j.1432-1033.1991.tb16475.x
– ident: e_1_2_5_133_2
  doi: 10.1023/A:1008367405025
– ident: e_1_2_5_53_2
  doi: 10.1021/ja00037a042
– ident: e_1_2_5_27_2
  doi: 10.1021/bi00245a008
– ident: e_1_2_5_95_2
  doi: 10.1007/BF00178258
– ident: e_1_2_5_94_2
  doi: 10.1111/j.1432-1033.1993.tb17746.x
– ident: e_1_2_5_128_2
  doi: 10.1021/ja00308a042
– ident: e_1_2_5_42_2
  doi: 10.1021/ja9630553
– ident: e_1_2_5_71_2
  doi: 10.1007/BF02192814
– ident: e_1_2_5_117_2
– ident: e_1_2_5_97_2
  doi: 10.1046/j.1432-1327.1999.00767.x
– ident: e_1_2_5_122_2
  doi: 10.1023/A:1008340116418
– ident: e_1_2_5_18_2
  doi: 10.1002/pro.5560061205
– ident: e_1_2_5_158_2
  doi: 10.1023/A:1026737732576
– ident: e_1_2_5_61_2
  doi: 10.1016/0022-2364(70)90067-3
– volume: 2
  start-page: 9
  year: 2004
  ident: e_1_2_5_48_2
  publication-title: J. Biomol. NMR
  contributor:
    fullname: Vakonakis I.
– ident: e_1_2_5_50_2
  doi: 10.1016/0006-291X(66)90527-4
– ident: e_1_2_5_66_2
  doi: 10.1111/j.1432-1033.1984.tb07942.x
– ident: e_1_2_5_127_2
– ident: e_1_2_5_59_2
  doi: 10.1006/jmre.1997.1187
– ident: e_1_2_5_77_2
  doi: 10.1021/ja029286t
– ident: e_1_2_5_14_2
  doi: 10.1016/0022-2836(91)90884-9
– ident: e_1_2_5_47_2
  doi: 10.1021/ja00004a075
– ident: e_1_2_5_68_2
  doi: 10.1021/bi00370a010
– ident: e_1_2_5_147_2
  doi: 10.1073/pnas.94.23.12366
– ident: e_1_2_5_70_2
  doi: 10.1021/ja00038a084
– start-page: 389
  volume-title: Chemistry and Biochemistry of Flavoenzymes
  year: 1992
  ident: e_1_2_5_5_2
  contributor:
    fullname: Mayhew S. G.
– start-page: 1504
  year: 2001
  ident: e_1_2_5_121_2
  publication-title: Biochim. Biophys. Acta
  contributor:
    fullname: Chang F.‐C.
– ident: e_1_2_5_91_2
  doi: 10.1021/ja001345k
– ident: e_1_2_5_73_2
  doi: 10.1073/pnas.95.24.14147
– ident: e_1_2_5_92_2
  doi: 10.1021/ja003080f
– ident: e_1_2_5_131_2
  doi: 10.1006/jmre.2000.2221
– ident: e_1_2_5_139_2
  doi: 10.1021/ja012674v
– ident: e_1_2_5_32_2
  doi: 10.1016/S0021-9258(18)96528-2
– ident: e_1_2_5_58_2
  doi: 10.1006/jmre.1996.7482
– ident: e_1_2_5_96_2
  doi: 10.1006/abbi.1994.1445
– ident: e_1_2_5_103_2
  doi: 10.1023/A:1008335502416
– ident: e_1_2_5_138_2
  doi: 10.1021/ja011618r
– ident: e_1_2_5_3_2
  doi: 10.1016/S1874-6047(08)60225-5
– ident: e_1_2_5_12_2
  doi: 10.1016/S0022-2836(83)80277-0
– ident: e_1_2_5_159_2
  doi: 10.1023/A:1011265430149
– ident: e_1_2_5_160_2
  doi: 10.1016/0009-2614(90)87025-M
– start-page: 427
  volume-title: Chemistry and Biochemistry of Flavoenzymes
  year: 1992
  ident: e_1_2_5_6_2
  contributor:
    fullname: Ludwig M. L.
– ident: e_1_2_5_74_2
  doi: 10.1021/ja983945d
– ident: e_1_2_5_67_2
  doi: 10.1111/j.1432-1033.1985.tb09067.x
– ident: e_1_2_5_152_2
  doi: 10.1021/ja982649y
– ident: e_1_2_5_57_2
– ident: e_1_2_5_17_2
  doi: 10.1111/j.1432-1033.1996.0190u.x
– ident: e_1_2_5_125_2
  doi: 10.1023/A:1022814324367
– ident: e_1_2_5_29_2
  doi: 10.1111/j.1432-1033.1996.0423z.x
– ident: e_1_2_5_104_2
  doi: 10.1021/ja9909024
– ident: e_1_2_5_60_2
– ident: e_1_2_5_89_2
  doi: 10.1021/ar010097
– ident: e_1_2_5_124_2
  doi: 10.1021/ja003724j
– ident: e_1_2_5_150_2
  doi: 10.1006/jmre.1998.1483
– ident: e_1_2_5_114_2
  doi: 10.1016/0022-2364(85)90122-2
– ident: e_1_2_5_26_2
  doi: 10.1021/bi00493a014
– ident: e_1_2_5_63_2
  doi: 10.1021/ja00106a046
– ident: e_1_2_5_75_2
  doi: 10.1021/ja9902221
– ident: e_1_2_5_132_2
  doi: 10.1023/A:1011250219293
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Snippet Hydrogen bonding plays a key role in the tight binding of the FMN cofactor and the regulation of its redox properties in flavodoxins. Hydrogen bonding...
Abstract Hydrogen bonding plays a key role in the tight binding of the FMN cofactor and the regulation of its redox properties in flavodoxins. Hydrogen bonding...
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SubjectTerms Apoproteins - chemistry
Apoproteins - metabolism
Desulfovibrio vulgaris
Desulfovibrio vulgaris - metabolism
flavin
Flavodoxin - chemistry
Flavodoxin - metabolism
Hydrogen Bonding
Models, Molecular
Molecular Structure
NMR spectroscopy
Nuclear Magnetic Resonance, Biomolecular - methods
Oxidation-Reduction
Protein Binding
protein structures
quantitative J correlation
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Structure-Activity Relationship
TROSY
Title Cofactor-Apoprotein Hydrogen Bonding in Oxidized and Fully Reduced Flavodoxin Monitored by Trans-Hydrogen-Bond Scalar Couplings
URI https://api.istex.fr/ark:/67375/WNG-RP7ZMNRZ-4/fulltext.pdf
https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fcbic.200400171
https://www.ncbi.nlm.nih.gov/pubmed/15515086
https://search.proquest.com/docview/21343720
https://search.proquest.com/docview/67064228
Volume 5
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