Wiring of Redox Enzymes on Three Dimensional Self-Assembled Molecular Scaffold

The integration of biological molecules and nanoscale components provides a fertile basis for the construction of hybrid materials of synergic properties and functions. Stable protein 1 (SP1), a highly stable ring shaped protein, was recently used to display different functional domains, to bind nan...

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Published inLangmuir Vol. 27; no. 20; pp. 12606 - 12613
Main Authors Frasconi, Marco, Heyman, Arnon, Medalsy, Izhar, Porath, Danny, Mazzei, Franco, Shoseyov, Oded
Format Journal Article
LanguageEnglish
Published Washington, DC American Chemical Society 18.10.2011
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Abstract The integration of biological molecules and nanoscale components provides a fertile basis for the construction of hybrid materials of synergic properties and functions. Stable protein 1 (SP1), a highly stable ring shaped protein, was recently used to display different functional domains, to bind nanoparticles (NPs), and to spontaneously form two and three-dimensional structures. Here we show an approach to wire redox enzymes on this self-assembled protein–nanoparticle hybrid. Those hybrids are genetically engineered SP1s, displaying glucose oxidase (GOx) enzymes tethered to the protein inner pore. Moreover, the Au-NP–protein hybrids self-assembled to multiple enzymatic layers on the surface. By wiring the redox enzymes to the electrode, we present an active structure for the bioelectrocatalytic oxidation of glucose. This system demonstrates for the first time a three-dimensional assembly of multiple catalytic modules on a protein scaffold with an efficient electrical wiring of the enzyme units on an electrode surface, thus implementing a hybrid electrically active unit for nanobioelectronic applications.
AbstractList The integration of biological molecules and nanoscale components provides a fertile basis for the construction of hybrid materials of synergic properties and functions. Stable protein 1 (SP1), a highly stable ring shaped protein, was recently used to display different functional domains, to bind nanoparticles (NPs), and to spontaneously form two and three-dimensional structures. Here we show an approach to wire redox enzymes on this self-assembled protein-nanoparticle hybrid. Those hybrids are genetically engineered SP1s, displaying glucose oxidase (GOx) enzymes tethered to the protein inner pore. Moreover, the Au-NP-protein hybrids self-assembled to multiple enzymatic layers on the surface. By wiring the redox enzymes to the electrode, we present an active structure for the bioelectrocatalytic oxidation of glucose. This system demonstrates for the first time a three-dimensional assembly of multiple catalytic modules on a protein scaffold with an efficient electrical wiring of the enzyme units on an electrode surface, thus implementing a hybrid electrically active unit for nanobioelectronic applications.
Author Medalsy, Izhar
Heyman, Arnon
Frasconi, Marco
Shoseyov, Oded
Porath, Danny
Mazzei, Franco
AuthorAffiliation “Sapienza” University of Rome
The Hebrew University of Jerusalem
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  givenname: Marco
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Cites_doi 10.1021/la7031972
10.1038/nnano.2009.354
10.1002/adma.200400088
10.1021/j100168a046
10.1007/s00216-010-3708-6
10.1039/b313149a
10.1021/ja052841h
10.1126/science.298.5602.2407
10.1021/cr068077e
10.1002/anie.200903075
10.1126/science.1080664
10.1002/chem.200601793
10.1021/ja00004a048
10.1021/ar7002804
10.1021/cr068069y
10.1002/anie.200902191
10.1021/nl070450q
10.1021/ja900718m
10.1016/j.jbiotec.2007.07.940
10.1104/pp.002436
10.1002/fuce.200800115
10.1021/ac0521100
10.1021/ac0605492
10.1039/c001965h
10.1021/nl900302z
10.1002/anie.200600394
10.1016/j.bios.2008.04.024
10.1016/S0021-9258(17)34643-4
10.1038/nmat775
10.1046/j.1365-313X.1993.04050887.x
10.1038/nmat2162
10.1038/nmat2496
10.1002/1521-3773(20011119)40:22<4128::AID-ANIE4128>3.0.CO;2-S
10.1038/nature06451
10.1002/anie.200903463
10.1002/smll.200500231
10.1016/j.colsurfb.2010.10.012
10.1126/science.1150421
10.1002/anie.200400651
10.1002/fuce.200800037
10.1021/ac060551t
10.1021/cr068123a
10.1002/adma.19930051206
10.1021/cr0300789
10.1021/nl048547p
10.1002/adma.200900487
10.1021/ar00173a002
10.1021/jp1014725
10.1063/1.2739537
10.1074/jbc.M409952200
10.1126/science.1070821
10.1016/j.jbiotec.2010.04.012
10.1002/adma.200501865
10.1038/nnano.2010.62
10.1021/cr020719k
10.1021/nl072455t
10.1021/jp991889c
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Issue 20
Keywords Self assembly
Glucose oxidase
Catalytic reaction
Enzyme
Nanoparticle
Hybrid material
Two dimensional structure
Multiple layer
Wire
Porous material
Protein
Electrodes
Pore
Three dimensional structure
Oxidation
Oxidoreductases
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2011 American Chemical Society
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References Murray R. W. (ref20/cit20b) 2008; 108
Yin P. (ref3/cit3c) 2008; 451
Olson P. D. (ref15/cit15) 1993; 4
Heller A. (ref5/cit5b) 2004; 6
Zhou N. (ref18/cit18b) 2006; 78
Chen H.-A. (ref21/cit21b) 2010; 114
Medalsy I. (ref13/cit13c) 2010; 5
Willner I. (ref5/cit5a) 2009; 9
Vamvakaki V. (ref9/cit9a) 2006; 78
Willner I. (ref6/cit6c) 1993; 5
Xiao Y. (ref8/cit8a) 2003; 299
Fruk L. (ref10/cit10b) 2007; 13
Jain P. K. (ref22/cit22a) 2008; 41
Zayats M. (ref8/cit8b) 2005; 127
Grueninger D. G. (ref3/cit3a) 2008; 319
Wang J. (ref4/cit4d) 2008; 108
Wang J. (ref19/cit19b) 2006; 2
Kavanagh P. (ref5/cit5d) 2009; 9
Calabrese Barton S. (ref5/cit5c) 2004; 104
Sukharev M. (ref20/cit20c) 2007; 126
Katz E. (ref4/cit4a) 2004; 43
Heyman A. (ref11/cit11b) 2007; 131
Heyman A. (ref11/cit11a) 2007; 7
Zhang H. (ref17/cit17b) 2011; 82
Wang W.-X. (ref12/cit12b) 2002; 130
Shuhmann W. (ref6/cit6b) 1991; 113
Mann S. (ref1/cit1a) 2009; 8
Whitesides G. M. (ref1/cit1b) 2002; 295
Welte L. (ref2/cit2a) 2010; 5
Willner O. I. (ref18/cit18c) 2009; 9
Heller A. (ref4/cit4e) 2008; 108
Boland S. (ref6/cit6d) 2008; 24
Frasconi M. (ref16/cit16b) 2010; 398
Zayats M. (ref17/cit17a) 2005; 5
Niemeyer C. M. (ref4/cit4b) 2001; 40
Love J. C. (ref16/cit16a) 2005; 105
Heyman A. (ref14/cit14) 2009; 48
Mas-Ballesté R. (ref2/cit2b) 2010; 39
Kavanagh P. (ref7/cit7b) 2006; 78
Brun M. (ref2/cit2c) 2004; 16
Morais S. (ref11/cit11c) 2010; 147
Heller A. (ref6/cit6a) 1990; 23
Willner I. (ref18/cit18a) 2006; 18
Gregg B. A. (ref7/cit7a) 1991; 95
Templeton A. C. (ref20/cit20a) 2000; 104
Yang W. (ref9/cit9b) 2010; 49
Behrens S. (ref13/cit13a) 2009; 21
Stankovich M. T. (ref23/cit23) 1978; 253
Anker J. N. (ref22/cit22b) 2008; 7
Courjean O. (ref24/cit24) 2009; 48
McMillan R. A. (ref3/cit3b) 2002; 1
Piperberg G. (ref10/cit10a) 2009; 131
Sheng Q. (ref19/cit19a) 2008; 24
Willner I. (ref4/cit4c) 2002; 298
Xu Q. (ref21/cit21a) 2006; 45
Madalsy I. (ref13/cit13b) 2008; 8
Dgany O. (ref12/cit12a) 2004; 279
References_xml – volume: 24
  start-page: 6351
  year: 2008
  ident: ref6/cit6d
  publication-title: Langmuir
  doi: 10.1021/la7031972
  contributor:
    fullname: Boland S.
– volume: 5
  start-page: 110
  year: 2010
  ident: ref2/cit2a
  publication-title: Nat. Nanotechnol.
  doi: 10.1038/nnano.2009.354
  contributor:
    fullname: Welte L.
– volume: 16
  start-page: 2087
  year: 2004
  ident: ref2/cit2c
  publication-title: Adv. Mater.
  doi: 10.1002/adma.200400088
  contributor:
    fullname: Brun M.
– volume: 95
  start-page: 5970
  year: 1991
  ident: ref7/cit7a
  publication-title: J. Phys. Chem.
  doi: 10.1021/j100168a046
  contributor:
    fullname: Gregg B. A.
– volume: 398
  start-page: 1545
  year: 2010
  ident: ref16/cit16b
  publication-title: Anal. Bioanal. Chem.
  doi: 10.1007/s00216-010-3708-6
  contributor:
    fullname: Frasconi M.
– volume: 6
  start-page: 209
  year: 2004
  ident: ref5/cit5b
  publication-title: Phys. Chem. Chem. Phys.
  doi: 10.1039/b313149a
  contributor:
    fullname: Heller A.
– volume: 127
  start-page: 12400
  year: 2005
  ident: ref8/cit8b
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja052841h
  contributor:
    fullname: Zayats M.
– volume: 298
  start-page: 2407
  year: 2002
  ident: ref4/cit4c
  publication-title: Science
  doi: 10.1126/science.298.5602.2407
  contributor:
    fullname: Willner I.
– volume: 108
  start-page: 2688
  year: 2008
  ident: ref20/cit20b
  publication-title: Chem. Rev.
  doi: 10.1021/cr068077e
  contributor:
    fullname: Murray R. W.
– volume: 48
  start-page: 9290
  year: 2009
  ident: ref14/cit14
  publication-title: Angew. Chem., Int. Ed.
  doi: 10.1002/anie.200903075
  contributor:
    fullname: Heyman A.
– volume: 299
  start-page: 1877
  year: 2003
  ident: ref8/cit8a
  publication-title: Science
  doi: 10.1126/science.1080664
  contributor:
    fullname: Xiao Y.
– volume: 13
  start-page: 5223
  year: 2007
  ident: ref10/cit10b
  publication-title: Chem.—Eur. J.
  doi: 10.1002/chem.200601793
  contributor:
    fullname: Fruk L.
– volume: 113
  start-page: 1394
  year: 1991
  ident: ref6/cit6b
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja00004a048
  contributor:
    fullname: Shuhmann W.
– volume: 41
  start-page: 1578
  year: 2008
  ident: ref22/cit22a
  publication-title: Acc. Chem. Res.
  doi: 10.1021/ar7002804
  contributor:
    fullname: Jain P. K.
– volume: 108
  start-page: 2482
  year: 2008
  ident: ref4/cit4e
  publication-title: Chem. Rev.
  doi: 10.1021/cr068069y
  contributor:
    fullname: Heller A.
– volume: 48
  start-page: 5897
  year: 2009
  ident: ref24/cit24
  publication-title: Angew. Chem., Int. Ed.
  doi: 10.1002/anie.200902191
  contributor:
    fullname: Courjean O.
– volume: 7
  start-page: 1575
  year: 2007
  ident: ref11/cit11a
  publication-title: Nano Lett.
  doi: 10.1021/nl070450q
  contributor:
    fullname: Heyman A.
– volume: 131
  start-page: 8724
  year: 2009
  ident: ref10/cit10a
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja900718m
  contributor:
    fullname: Piperberg G.
– volume: 131
  start-page: 433
  year: 2007
  ident: ref11/cit11b
  publication-title: J. Biotechnol.
  doi: 10.1016/j.jbiotec.2007.07.940
  contributor:
    fullname: Heyman A.
– volume: 130
  start-page: 865
  year: 2002
  ident: ref12/cit12b
  publication-title: Plant Physiol.
  doi: 10.1104/pp.002436
  contributor:
    fullname: Wang W.-X.
– volume: 9
  start-page: 7
  year: 2009
  ident: ref5/cit5a
  publication-title: Fuel Cells
  doi: 10.1002/fuce.200800115
  contributor:
    fullname: Willner I.
– volume: 78
  start-page: 2710
  year: 2006
  ident: ref7/cit7b
  publication-title: Anal. Chem.
  doi: 10.1021/ac0521100
  contributor:
    fullname: Kavanagh P.
– volume: 78
  start-page: 5227
  year: 2006
  ident: ref18/cit18b
  publication-title: Anal. Chem.
  doi: 10.1021/ac0605492
  contributor:
    fullname: Zhou N.
– volume: 39
  start-page: 4220
  year: 2010
  ident: ref2/cit2b
  publication-title: Chem. Soc. Rev.
  doi: 10.1039/c001965h
  contributor:
    fullname: Mas-Ballesté R.
– volume: 9
  start-page: 2040
  year: 2009
  ident: ref18/cit18c
  publication-title: Nano Lett.
  doi: 10.1021/nl900302z
  contributor:
    fullname: Willner O. I.
– volume: 45
  start-page: 3631
  year: 2006
  ident: ref21/cit21a
  publication-title: Angew. Chem., Int. Ed.
  doi: 10.1002/anie.200600394
  contributor:
    fullname: Xu Q.
– volume: 24
  start-page: 429
  year: 2008
  ident: ref19/cit19a
  publication-title: Biosens. Bioelectron.
  doi: 10.1016/j.bios.2008.04.024
  contributor:
    fullname: Sheng Q.
– volume: 253
  start-page: 4971
  year: 1978
  ident: ref23/cit23
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(17)34643-4
  contributor:
    fullname: Stankovich M. T.
– volume: 1
  start-page: 247
  year: 2002
  ident: ref3/cit3b
  publication-title: Nat. Mater.
  doi: 10.1038/nmat775
  contributor:
    fullname: McMillan R. A.
– volume: 4
  start-page: 887
  year: 1993
  ident: ref15/cit15
  publication-title: Plant J.
  doi: 10.1046/j.1365-313X.1993.04050887.x
  contributor:
    fullname: Olson P. D.
– volume: 7
  start-page: 442
  year: 2008
  ident: ref22/cit22b
  publication-title: Nat. Mater.
  doi: 10.1038/nmat2162
  contributor:
    fullname: Anker J. N.
– volume: 8
  start-page: 781
  year: 2009
  ident: ref1/cit1a
  publication-title: Nat. Mater.
  doi: 10.1038/nmat2496
  contributor:
    fullname: Mann S.
– volume: 40
  start-page: 4128
  year: 2001
  ident: ref4/cit4b
  publication-title: Angew. Chem., Int. Ed.
  doi: 10.1002/1521-3773(20011119)40:22<4128::AID-ANIE4128>3.0.CO;2-S
  contributor:
    fullname: Niemeyer C. M.
– volume: 451
  start-page: 318
  year: 2008
  ident: ref3/cit3c
  publication-title: Nature
  doi: 10.1038/nature06451
  contributor:
    fullname: Yin P.
– volume: 49
  start-page: 2114
  year: 2010
  ident: ref9/cit9b
  publication-title: Angew. Chem., Int. Ed.
  doi: 10.1002/anie.200903463
  contributor:
    fullname: Yang W.
– volume: 2
  start-page: 129
  year: 2006
  ident: ref19/cit19b
  publication-title: Small
  doi: 10.1002/smll.200500231
  contributor:
    fullname: Wang J.
– volume: 82
  start-page: 532
  year: 2011
  ident: ref17/cit17b
  publication-title: Colloids Surf., B
  doi: 10.1016/j.colsurfb.2010.10.012
  contributor:
    fullname: Zhang H.
– volume: 319
  start-page: 206
  year: 2008
  ident: ref3/cit3a
  publication-title: Science
  doi: 10.1126/science.1150421
  contributor:
    fullname: Grueninger D. G.
– volume: 43
  start-page: 6042
  year: 2004
  ident: ref4/cit4a
  publication-title: Angew. Chem., Int. Ed.
  doi: 10.1002/anie.200400651
  contributor:
    fullname: Katz E.
– volume: 9
  start-page: 79
  year: 2009
  ident: ref5/cit5d
  publication-title: Fuel Cells
  doi: 10.1002/fuce.200800037
  contributor:
    fullname: Kavanagh P.
– volume: 78
  start-page: 5538
  year: 2006
  ident: ref9/cit9a
  publication-title: Anal. Chem.
  doi: 10.1021/ac060551t
  contributor:
    fullname: Vamvakaki V.
– volume: 108
  start-page: 814
  year: 2008
  ident: ref4/cit4d
  publication-title: Chem. Rev.
  doi: 10.1021/cr068123a
  contributor:
    fullname: Wang J.
– volume: 5
  start-page: 912
  year: 1993
  ident: ref6/cit6c
  publication-title: Adv. Mater.
  doi: 10.1002/adma.19930051206
  contributor:
    fullname: Willner I.
– volume: 105
  start-page: 1103
  year: 2005
  ident: ref16/cit16a
  publication-title: Chem. Rev.
  doi: 10.1021/cr0300789
  contributor:
    fullname: Love J. C.
– volume: 5
  start-page: 21
  year: 2005
  ident: ref17/cit17a
  publication-title: Nano Lett.
  doi: 10.1021/nl048547p
  contributor:
    fullname: Zayats M.
– volume: 21
  start-page: 3515
  year: 2009
  ident: ref13/cit13a
  publication-title: Adv. Mater.
  doi: 10.1002/adma.200900487
  contributor:
    fullname: Behrens S.
– volume: 23
  start-page: 128
  year: 1990
  ident: ref6/cit6a
  publication-title: Acc. Chem. Res.
  doi: 10.1021/ar00173a002
  contributor:
    fullname: Heller A.
– volume: 114
  start-page: 10359
  year: 2010
  ident: ref21/cit21b
  publication-title: J. Phys. Chem. C
  doi: 10.1021/jp1014725
  contributor:
    fullname: Chen H.-A.
– volume: 126
  start-page: 204702
  year: 2007
  ident: ref20/cit20c
  publication-title: J. Chem. Phys.
  doi: 10.1063/1.2739537
  contributor:
    fullname: Sukharev M.
– volume: 279
  start-page: 51516
  year: 2004
  ident: ref12/cit12a
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M409952200
  contributor:
    fullname: Dgany O.
– volume: 295
  start-page: 2418
  year: 2002
  ident: ref1/cit1b
  publication-title: Science
  doi: 10.1126/science.1070821
  contributor:
    fullname: Whitesides G. M.
– volume: 147
  start-page: 205
  year: 2010
  ident: ref11/cit11c
  publication-title: J. Biotechnol.
  doi: 10.1016/j.jbiotec.2010.04.012
  contributor:
    fullname: Morais S.
– volume: 18
  start-page: 1109
  year: 2006
  ident: ref18/cit18a
  publication-title: Adv. Mater.
  doi: 10.1002/adma.200501865
  contributor:
    fullname: Willner I.
– volume: 5
  start-page: 451
  year: 2010
  ident: ref13/cit13c
  publication-title: Nat. Nanotechnol.
  doi: 10.1038/nnano.2010.62
  contributor:
    fullname: Medalsy I.
– volume: 104
  start-page: 4867
  year: 2004
  ident: ref5/cit5c
  publication-title: Chem. Rev.
  doi: 10.1021/cr020719k
  contributor:
    fullname: Calabrese Barton S.
– volume: 8
  start-page: 473
  year: 2008
  ident: ref13/cit13b
  publication-title: Nano Lett.
  doi: 10.1021/nl072455t
  contributor:
    fullname: Madalsy I.
– volume: 104
  start-page: 564
  year: 2000
  ident: ref20/cit20a
  publication-title: Phys. Chem. B
  doi: 10.1021/jp991889c
  contributor:
    fullname: Templeton A. C.
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Snippet The integration of biological molecules and nanoscale components provides a fertile basis for the construction of hybrid materials of synergic properties and...
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SubjectTerms Catalysis
Chemistry
Colloidal state and disperse state
Exact sciences and technology
General and physical chemistry
Glucose Oxidase - chemistry
Gold - chemistry
Materials: Nano-and Mesostructured Materials, Polymers, Gels, Liquid Crystals, Composites
Metal Nanoparticles - chemistry
Microscopy, Atomic Force
Models, Molecular
Oxidation-Reduction
Physical and chemical studies. Granulometry. Electrokinetic phenomena
Porous materials
Sulfhydryl Compounds - chemistry
Theory of reactions, general kinetics. Catalysis. Nomenclature, chemical documentation, computer chemistry
Title Wiring of Redox Enzymes on Three Dimensional Self-Assembled Molecular Scaffold
URI http://dx.doi.org/10.1021/la2020435
https://www.ncbi.nlm.nih.gov/pubmed/21895003
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Volume 27
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