Biochemical characterization of NADH:FMN oxidoreductase HcbA3 from Nocardioides sp. PD653 in catalyzing aerobic HCB dechlorination
Nocardioides sp. PD653 genes hcbA1, hcbA2, and hcbA3 encode enzymes that catalyze the oxidative dehalogenation of hexachlorobenzene (HCB), which is one of the most recalcitrant persistent organic pollutants (POPs). In this study, HcbA1, HcbA2, and HcbA3 were heterologously expressed and characterize...
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| Published in | Journal of Pesticide Science Vol. 45; no. 3; pp. 125 - 131 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
Tokyo
Pesticide Science Society of Japan
20.08.2020
Japan Science and Technology Agency |
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| Abstract | Nocardioides sp. PD653 genes hcbA1, hcbA2, and hcbA3 encode enzymes that catalyze the oxidative dehalogenation of hexachlorobenzene (HCB), which is one of the most recalcitrant persistent organic pollutants (POPs). In this study, HcbA1, HcbA2, and HcbA3 were heterologously expressed and characterized. Among the flavin species tested, HcbA3 showed the highest affinity for FMN with a Kd value of 0.75±0.17 µM. Kinetic assays revealed that HcbA3 followed a ping-pong bi–bi mechanism for the reduction of flavins. The Km for NADH and FMN was 51.66±11.58 µM and 4.43±0.69 µM, respectively. For both NADH and FMN, the Vmax and kcat were 2.21±0.86 µM and 66.74±5.91 sec−1, respectively. We also successfully reconstituted the oxidative dehalogenase reaction in vitro, which consisted of HcbA1, HcbA3, FMN, and NADH, suggesting that HcbA3 may be the partner reductase component for HcbA1 in Nocardioides sp. PD653. |
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| AbstractList | Nocardioides sp. PD653 genes hcbA1, hcbA2, and hcbA3 encode enzymes that catalyze the oxidative dehalogenation of hexachlorobenzene (HCB), which is one of the most recalcitrant persistent organic pollutants (POPs). In this study, HcbA1, HcbA2, and HcbA3 were heterologously expressed and characterized. Among the flavin species tested, HcbA3 showed the highest affinity for FMN with a Kd value of 0.75±0.17 µM. Kinetic assays revealed that HcbA3 followed a ping-pong bi–bi mechanism for the reduction of flavins. The Km for NADH and FMN was 51.66±11.58 µM and 4.43±0.69 µM, respectively. For both NADH and FMN, the Vmax and kcat were 2.21±0.86 µM and 66.74±5.91 sec−1, respectively. We also successfully reconstituted the oxidative dehalogenase reaction in vitro, which consisted of HcbA1, HcbA3, FMN, and NADH, suggesting that HcbA3 may be the partner reductase component for HcbA1 in Nocardioides sp. PD653. Nocardioides sp. PD653 genes hcbA1, hcbA2, and hcbA3 encode enzymes that catalyze the oxidative dehalogenation of hexachlorobenzene (HCB), which is one of the most recalcitrant persistent organic pollutants (POPs). In this study, HcbA1, HcbA2, and HcbA3 were heterologously expressed and characterized. Among the flavin species tested, HcbA3 showed the highest affinity for FMN with a Kd value of 0.75 +- 0.17μM. Kinetic assays revealed that HcbA3 followed a ping-pong bi-bi mechanism for the reduction of flavins. The Km for NADH and FMN was 51.66 +- 11.58μM and 4.43 +- 0.69μM, respectively. For both NADH and FMN, the Vmax and kcat were 2.21 +- 0.86μM and 66.74 +- 5.91sec-1, respectively. We also successfully reconstituted the oxidative dehalogenase reaction in vitro, which consisted of HcbA1, HcbA3, FMN, and NADH, suggesting that HcbA3 may be the partner reductase component for HcbA1 in Nocardioides sp. PD653. Nocardioides sp. PD653 genes hcbA1 , hcbA2 , and hcbA3 encode enzymes that catalyze the oxidative dehalogenation of hexachlorobenzene (HCB), which is one of the most recalcitrant persistent organic pollutants (POPs). In this study, HcbA1, HcbA2, and HcbA3 were heterologously expressed and characterized. Among the flavin species tested, HcbA3 showed the highest affinity for FMN with a K d value of 0.75±0.17 µM. Kinetic assays revealed that HcbA3 followed a ping-pong bi–bi mechanism for the reduction of flavins. The K m for NADH and FMN was 51.66±11.58 µM and 4.43±0.69 µM, respectively. For both NADH and FMN, the V max and k cat were 2.21±0.86 µM and 66.74±5.91 sec −1 , respectively. We also successfully reconstituted the oxidative dehalogenase reaction in vitro , which consisted of HcbA1, HcbA3, FMN, and NADH, suggesting that HcbA3 may be the partner reductase component for HcbA1 in Nocardioides sp. PD653. |
| Author | Ito, Koji Kiyota, Hiromasa Takagi, Kazuhiro Kataoka, Ryota |
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| Cites_doi | 10.1128/JB.00966-06 10.1562/0031-8655(2003)077<0446:ETEFIV>2.0.CO;2 10.1007/s00253-015-6872-y 10.1023/A:1005175106042 10.1128/JB.182.3.627-636.2000 10.1074/jbc.270.29.17339 10.1016/j.abb.2013.12.005 10.1016/S0021-9258(18)35687-4 10.1128/JB.174.4.1179-1188.1992 10.1016/j.bbrep.2015.09.005 10.1128/AEM.67.2.688-695.2001 10.1074/jbc.274.38.26639 10.1074/jbc.M209689200 10.1128/AEM.72.5.3524-3530.2006 10.1074/jbc.M109.056135 10.1128/JB.179.4.1112-1116.1997 10.1042/BSR20140060 10.1074/jbc.M307397200 10.1093/nar/7.6.1513 10.1128/AEM.02329-08 10.1128/MMBR.55.1.123-142.1991 10.1016/j.bbrc.2005.04.033 10.1128/JB.01050-07 10.1111/j.1440-1681.2004.04088.x 10.1128/JB.185.9.2786-2792.2003 10.1021/bi981841+ 10.1128/AEM.66.2.481-486.2000 10.1128/JB.178.21.6123-6132.1996 10.1074/jbc.M709730200 10.1007/s12088-008-0007-4 10.1016/j.scitotenv.2005.03.014 10.1128/AEM.00824-17 10.1016/S1369-5274(03)00065-1 10.1074/jbc.274.41.29358 10.1021/acs.biochem.9b00012 |
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| References | 20) J. Valton, C. Mathevon, M. Fontecave, V. Niviére and D. P. Ballou: J. Biol. Chem. 283, 10287–10296 (2008). 23) M. R. Gisi and L. Xun: J. Bacteriol. 185, 2786–2792 (2003). 3) K. Ito, K. Takagi, A. Iwasaki, N. Tanaka, Y. Kanesaki, F. Martin-Laurent and S. Igimi: Appl. Environ. Microbiol. 83, e00824–e17 (2017). 18) S. G. Kendrew, S. E. Harding, D. A. Hopwood and E. N. Marsh: J. Biol. Chem. 270, 17339–17343 (1995). 8) Y. Okegawa and K. Motohashi: Biochem. Biophys. Rep. 4, 148–151 (2015). 11) U. Arunachalam, V. Massey and C. S. Vaidyanathan: J. Biol. Chem. 267, 25848–25855 (1992). 25) U. Kirchner, A. H. Westphal, R. Müller and J. H. van Berkel: J. Biol. Chem. 279, 47545–47553 (2003). 35) R. J. Russell, R. L. Harcourt and J. G. Oakshott: ACIAR Proc. 85, 341-348 (1998). 14) Y. Xu, M. W. Mortimer, T. S. Fisher, M. L. Kahn, F. J. Brockman and L. Xun: J. Bacteriol. 179, 1112–1116 (1997). 2) K. Takagi, A. Iwasaki, I. Kamei, K. Satsuma, Y. Yoshioka and N. Harada: Appl. Environ. Microbiol. 75, 4452–4458 (2009). 1) J. L. Barber, A. J. Sweetman, D. van Wijk and K. C. Jones: Sci. Total Environ. 349, 1–44 (2005). 7) S. Adak and T. P. Begley: Biochemistry 58, 1181–1183 (2019). 13) H. R. Knobel, T. Egli and J. R. van der Meer: J. Bacteriol. 178, 6123–6132 (1996). 17) E. Eichhorn, J. R. van der Ploeg and T. Leisinger: J. Biol. Chem. 274, 26639–26646 (1999). 31) J. K. Lee and H. Zhao: J. Bacteriol. 189, 8556–8563 (2007). 5) M. M. E. Huijbers, S. Montersino, A. H. Westphal, D. Tischler and W. J. H. van Berkel: Arch. Biochem. Biophys. 544, 2–17 (2014). 15) K. A. Gray, G. T. Mrachko and C. H. Squires: Curr. Opin. Microbiol. 6, 229–235 (2003). 9) B. Gao and H. R. Ellis: Biochem. Biophys. Res. Commun. 331, 1137–1145 (2005). 6) L. Xun and E. R. Sandvik: Appl. Environ. Microbiol. 66, 481–486 (2000). 21) K. M. Weir, T. D. Sutherland, I. Horne, R. J. Russell and J. G. Oakeshott: Appl. Environ. Microbiol. 72, 3524–3530 (2006). 28) B. Lei and S. C. Tu: Biochemistry 37, 14623–14629 (1998). 19) L. Filisetti, M. Fontecave and V. Niviére: J. Biol. Chem. 278, 296–303 (2003). 29) J. C. Low and S. C. Tu: Photochem. Photobiol. 77, 446–452 (2003). 26) A. D. Lawrence, S. L. Taylor, A. Scott, M. L. Rowe, C. M. Johnson, S. E. J. Rigby, M. A. Geeves, R. W. Pickersgill, M. J. Howard and M. J. Warren: Biosci. Rep. 34, e00120 (2014). 4) H. R. Ellis: Arch. Biochem. Biophys. 497, 1–12 (2010). 27) B. N. Webb, J. W. Ballinger, E. Kim, S. M. Belchik, K. S. Lam, B. Youn, M. S. Nissen, L. Xun and C. Kang: J. Biol. Chem. 285, 2014–2027 (2010). 24) B. Galán, E. Díaz, M. A. Prieto and J. L. García: J. Bacteriol. 182, 627–636 (2000). 34) T. D. Sutherland, I. Horne, K. M. Weir, C. W. Coppin, M. R. Williams, M. Selleck, R. J. Russell and J. G. Oakshott: Clin. Exp. Pharmacol. Physiol. 31, 817–821 (2004). 22) J. Bohuslavek, J. W. Payne, Y. Liu, H. J. Bolton Jr. and L. Xun: Appl. Environ. Microbiol. 67, 688–695 (2001). 10) E. A. Meighen: Microbiol. Rev. 55, 123–142 (1991). 12) T. Uetz, R. Schneider, M. Snozzi and T. Egli: J. Bacteriol. 174, 1179–1188 (1992). 36) H. C. Birnboim and J. Doly: Nucleic Acids Res. 7, 1513–1523 (1979). 33) C. Scott, G. Pandey, C. Hartley, C. Jackson, M. Cheesman, M. Taylor, R. Pandey, J. Khurana, M. Teese, C. Coppin, K. Weir, R. Jain, R. Lal, R. Russell and J. Oakeshott: Indian J. Microbiol. 48, 65–79 (2008). 16) J. R. van der Ploeg, R. Iwanicka-Nowicka, T. Bykowski, M. M. Hryniewicz and T. Leisinger: J. Biol. Chem. 274, 29358–29365 (1999). 30) K. Abdurachim and H. R. Ellis: J. Bacteriol. 188, 8153–8159 (2006). 32) G. Eibes, A. Arca-Ramos, G. Feijoo, J. M. Lema and M. T. Moreira: Appl. Microbiol. Biotechnol. 99, 8815–8829 (2015). 22 23 24 25 26 27 28 29 30 31 10 32 11 33 12 34 13 35 14 36 15 16 17 18 19 1 2 3 4 5 6 7 8 9 20 21 |
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| Snippet | Nocardioides sp. PD653 genes hcbA1, hcbA2, and hcbA3 encode enzymes that catalyze the oxidative dehalogenation of hexachlorobenzene (HCB), which is one of the... Nocardioides sp. PD653 genes hcbA1 , hcbA2 , and hcbA3 encode enzymes that catalyze the oxidative dehalogenation of hexachlorobenzene (HCB), which is one of... |
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| SubjectTerms | Dechlorination Dehalogenation Flavin mononucleotide flavin reductase HcbA3 Hexachlorobenzene NADH Nicotinamide adenine dinucleotide Nocardioides sp. PD653 Original Oxidoreductase Persistent organic pollutants Pollutants Reductases TC-FDM |
| Title | Biochemical characterization of NADH:FMN oxidoreductase HcbA3 from Nocardioides sp. PD653 in catalyzing aerobic HCB dechlorination |
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