메뉴 건너뛰기




Volumn 367, Issue 1593, 2012, Pages 1204-1212

Biochemical characterization of the purple form of Marinobacter hydrocarbonoclasticus nitrous oxide reductase

Author keywords

Denitrification; Fully oxidized CuZ centre; Isolation in presence of oxygen; Marinobacter; Nitrous oxide reductase; Purple form

Indexed keywords

BACTERIUM; BIOCHEMISTRY; BIOTECHNOLOGY; CATALYSIS; DENITRIFICATION; ENZYME ACTIVITY; MARINE TECHNOLOGY; NITRATE; NITROUS OXIDE; REDOX CONDITIONS; REDUCTION; SULFUR;

EID: 84859067712     PISSN: 09628436     EISSN: 14712970     Source Type: Journal    
DOI: 10.1098/rstb.2011.0311     Document Type: Article
Times cited : (26)

References (38)
  • 2
    • 34249813395 scopus 로고    scopus 로고
    • Biogeochemical simulation of nitrous oxide cycle based on the major nitrogen processes
    • (doi:10.1029/2005jg000109)
    • Sorai, M., Yoshida, N. & Ishikawa, M. 2007 Biogeochemical simulation of nitrous oxide cycle based on the major nitrogen processes. J. Geophys. Res. 112, G01006. (doi:10.1029/2005jg000109)
    • (2007) J. Geophys. Res. , vol.112
    • Sorai, M.1    Yoshida, N.2    Ishikawa, M.3
  • 3
    • 0002951380 scopus 로고
    • Aspects of the marine nitrogen cycle with relevance to the dynamics of nitrous and nitric oxide
    • In, (eds J. E. Roders & W. E. Whitman), Washington, DC: American Society of Microbiology
    • Capone, D. G. 1991 Aspects of the marine nitrogen cycle with relevance to the dynamics of nitrous and nitric oxide. In Microbial production and consumption of greenhouse gases (eds J. E. Roders & W. E. Whitman), pp. 255-275. Washington, DC: American Society of Microbiology.
    • (1991) Microbial production and consumption of greenhouse gases , pp. 255-275
    • Capone, D.G.1
  • 5
    • 33749337025 scopus 로고    scopus 로고
    • 2O) to dinitrogen by Bacteria and Archaea
    • (doi:10.1016/S0065-2911(06)52003-X)
    • 2O) to dinitrogen by Bacteria and Archaea. Adv. Microb. Physiol. 52, 107-227. (doi:10.1016/S0065-2911(06)52003-X)
    • (2007) Adv. Microb. Physiol. , vol.52 , pp. 107-227
    • Zumft, W.G.1    Kroneck, P.M.2
  • 6
    • 0023046623 scopus 로고
    • 2O as a substrate and as a competitive inhibitor of nitrogenase
    • (doi:10.1021/bi00353a021)
    • 2O as a substrate and as a competitive inhibitor of nitrogenase. Biochemistry 25, 1083-1088. (doi:10.1021/bi00353a021)
    • (1986) Biochemistry , vol.25 , pp. 1083-1088
    • Jensen, B.1    Burris, R.2
  • 7
    • 0034680937 scopus 로고    scopus 로고
    • Competitive substrate and inhibitor interactions at the physiologically relevant active site of nitrogenase
    • (doi:10.1074/jbc. M004889200)
    • Christiansen, J., Seefeldt, L. C. & Dean, D. R. 2000 Competitive substrate and inhibitor interactions at the physiologically relevant active site of nitrogenase. J. Biol. Chem. 275, 36 104-36 107. (doi:10.1074/jbc. M004889200)
    • (2000) J. Biol. Chem. , vol.275 , pp. 36104-36107
    • Christiansen, J.1    Seefeldt, L.C.2    Dean, D.R.3
  • 8
    • 0027487996 scopus 로고
    • The reduction of nitrous oxide to dinitrogen by Escherichia coli
    • (doi:10.1007/BF00245303)
    • Kaldorf, M., Linne von Berg, K., Meier, U., Servos, U. & Bothe, H. 1993 The reduction of nitrous oxide to dinitrogen by Escherichia coli. Arch. Microbiol. 160, 432-439. (doi:10.1007/BF00245303)
    • (1993) Arch. Microbiol. , vol.160 , pp. 432-439
    • Kaldorf, M.1    von Berg Linne, K.2    Meier, U.3    Servos, U.4    Bothe, H.5
  • 9
    • 77954726299 scopus 로고    scopus 로고
    • The multicopper oxidase from the archaeon Pyrobaculum aerophilum shows nitrous oxide reductase activity
    • (doi:10.1111/j.1742-4658.2010.07725.x
    • Fernandes, A. T., Damas, J. M., Todorovic, S., Huber, R., Baratto, M. C., Pogni, R., Soares, C. M. & Martins, L. O. 2010 The multicopper oxidase from the archaeon Pyrobaculum aerophilum shows nitrous oxide reductase activity. FEBS J. 277, 3176-3189. (doi:10.1111/j.1742-4658.2010.07725.x
    • (2010) FEBS J. , vol.277 , pp. 3176-3189
    • Fernandes, A.T.1    Damas, J.M.2    Todorovic, S.3    Huber, R.4    Baratto, M.C.5    Pogni, R.6    Soares, C.M.7    Martins, L.O.8
  • 10
    • 0020420055 scopus 로고
    • A novel kind of multi-copper protein as terminal oxidoreductase of nitrous oxide respiration in Pseudomonas perfectomarinus
    • (doi:10.1016/0014-5793 (82)81253-2)
    • Zumft, W. G. & Matsubara, T. 1982 A novel kind of multi-copper protein as terminal oxidoreductase of nitrous oxide respiration in Pseudomonas perfectomarinus. FEBS Lett. 148, 107-112. (doi:10.1016/0014-5793 (82)81253-2)
    • (1982) FEBS Lett. , vol.148 , pp. 107-112
    • Zumft, W.G.1    Matsubara, T.2
  • 12
    • 0024964611 scopus 로고
    • The nature of the cupric site in nitrous oxide reductase and of CuA in cytochrome c oxidase
    • (doi:10.1016/0014-5793(89)80464-8)
    • Kroneck, P. M., Antholine, W. A., Riester, J. & Zumft, W. G. 1989 The nature of the cupric site in nitrous oxide reductase and of CuA in cytochrome c oxidase. FEBS Lett. 248, 212-213. (doi:10.1016/0014-5793(89)80464-8)
    • (1989) FEBS Lett. , vol.248 , pp. 212-213
    • Kroneck, P.M.1    Antholine, W.A.2    Riester, J.3    Zumft, W.G.4
  • 13
    • 0039454785 scopus 로고    scopus 로고
    • Note: Transfer of Pseudomonas nautica to Marinobacter hydrocarbonoclasticus
    • (doi:10. 1099/00207713-48-4-1445)
    • Sproer, C., Lang, E., Hobeck, P., Burghardt, J., Stackebrandt, E. & Tindall, B. J. 1998 Note: transfer of Pseudomonas nautica to Marinobacter hydrocarbonoclasticus. Int. J. Syst. Bacteriol. 48, 1445-1448. (doi:10. 1099/00207713-48-4-1445)
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 1445-1448
    • Sproer, C.1    Lang, E.2    Hobeck, P.3    Burghardt, J.4    Stackebrandt, E.5    Tindall, B.J.6
  • 14
    • 79951550671 scopus 로고    scopus 로고
    • The tetranuclear copper active site of nitrous oxide reductase: The CuZ center
    • (doi:10.1007/s00775-011-0753-3)
    • Dell'acqua, S., Pauleta, S., Moura, I. & Moura, J. J. G. 2011 The tetranuclear copper active site of nitrous oxide reductase: the CuZ center. J. Biol. Inorg. Chem. 16, 183-194. (doi:10.1007/s00775-011-0753-3)
    • (2011) J. Biol. Inorg. Chem. , vol.16 , pp. 183-194
    • Dell'acqua, S.1    Pauleta, S.2    Moura, I.3    Moura J.J., G.4
  • 15
    • 0037096979 scopus 로고    scopus 로고
    • Multiple forms of the catalytic centre, CuZ, in the enzyme nitrous oxide reductase from Paracoccus pantotrophus
    • (doi:10.1042/ BJ20020055)
    • Rasmussen, T., Berks, B. C., Butt, J. N. & Thomson, A. J. 2002 Multiple forms of the catalytic centre, CuZ, in the enzyme nitrous oxide reductase from Paracoccus pantotrophus. Biochem. J. 364, 807-815. (doi:10.1042/ BJ20020055)
    • (2002) Biochem. J. , vol.364 , pp. 807-815
    • Rasmussen, T.1    Berks, B.C.2    Butt, J.N.3    Thomson, A.J.4
  • 16
    • 0032543960 scopus 로고    scopus 로고
    • CuA and CuZ are variants of the electron transfer center in nitrous oxide reductase
    • (doi:10.1073/pnas.95.17.9891)
    • Farrar, J. A., Zumft, W. G. & Thomson, A. J. 1998 CuA and CuZ are variants of the electron transfer center in nitrous oxide reductase. Proc. Natl Acad. Sci USA 95, 9891-9896. (doi:10.1073/pnas.95.17.9891)
    • (1998) Proc. Natl Acad. Sci USA , vol.95 , pp. 9891-9896
    • Farrar, J.A.1    Zumft, W.G.2    Thomson, A.J.3
  • 17
    • 0039619862 scopus 로고    scopus 로고
    • Purification, characterization, and preliminary crystallographic study of copper-containing nitrous oxide reductase from Pseudomonas nautica 617
    • (doi:10.1021/ bi9926328)
    • Prudencio, M. et al. 2000 Purification, characterization, and preliminary crystallographic study of copper-containing nitrous oxide reductase from Pseudomonas nautica 617. Biochemistry 39, 3899-3907. (doi:10.1021/ bi9926328)
    • (2000) Biochemistry , vol.39 , pp. 3899-3907
    • Prudencio, M.1
  • 19
    • 1642407786 scopus 로고    scopus 로고
    • Reductively activated nitrous oxide reductase reacts directly with substrate
    • (doi:10.1021/ja0398868)
    • Chan, J. M., Bollinger, J. A., Grewell, C. L. & Dooley, D. M. 2004 Reductively activated nitrous oxide reductase reacts directly with substrate. J. Am. Chem. Soc. 126, 3030-3031. (doi:10.1021/ja0398868)
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3030-3031
    • Chan, J.M.1    Bollinger, J.A.2    Grewell, C.L.3    Dooley, D.M.4
  • 21
    • 0022336620 scopus 로고
    • Nitrous oxide reductase from denitrifying Pseudomonas perfectomarina. Purification and properties of a novel multicopper enzyme
    • (doi:10.1111/j.1432-1033.1985. tb09324.x)
    • Coyle, C. L., Zumft, W. G., Kroneck, P. M., Korner, H. & Jakob, W. 1985 Nitrous oxide reductase from denitrifying Pseudomonas perfectomarina. Purification and properties of a novel multicopper enzyme. Eur. J. Biochem. 153, 459-467. (doi:10.1111/j.1432-1033.1985. tb09324.x)
    • (1985) Eur. J. Biochem. , vol.153 , pp. 459-467
    • Coyle, C.L.1    Zumft, W.G.2    Kroneck, P.M.3    Korner, H.4    Jakob, W.5
  • 22
    • 0023654742 scopus 로고
    • Purification and some characteristics of nitrous oxide reductase from Paracoccus denitrificans
    • Snyder, S. W. & Hollocher, T. C. 1987 Purification and some characteristics of nitrous oxide reductase from Paracoccus denitrificans. J. Biol. Chem. 262, 6515-6525.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6515-6525
    • Snyder, S.W.1    Hollocher, T.C.2
  • 23
    • 0033083840 scopus 로고    scopus 로고
    • Biochemical characterization and solution structure of nitrous oxide reductase from Alcaligenes xylosoxidans (NCIMB 11015)
    • (doi:10.1046/j.1432-1327. 1999.00082.x)
    • Ferretti, S., Grossmann, J. G., Hasnain, S. S., Eady, R. R. & Smith, B. E. 1999 Biochemical characterization and solution structure of nitrous oxide reductase from Alcaligenes xylosoxidans (NCIMB 11015). Eur. J. Biochem. 259, 651-659. (doi:10.1046/j.1432-1327. 1999.00082.x)
    • (1999) Eur. J. Biochem. , vol.259 , pp. 651-659
    • Ferretti, S.1    Grossmann, J.G.2    Hasnain, S.S.3    Eady, R.R.4    Smith, B.E.5
  • 24
    • 0024959342 scopus 로고
    • Nitrous oxide reductase from Pseudomonas stutzeri. Redox properties and spectroscopic characterization of different forms of the multicopper enzyme
    • (doi:10.1111/j.1432-1033.1989.tb14506.x)
    • Riester, J., Zumft, W. G. & Kroneck, P. M. 1989 Nitrous oxide reductase from Pseudomonas stutzeri. Redox properties and spectroscopic characterization of different forms of the multicopper enzyme. Eur. J. Biochem. 178, 751-762. (doi:10.1111/j.1432-1033.1989.tb14506.x)
    • (1989) Eur. J. Biochem. , vol.178 , pp. 751-762
    • Riester, J.1    Zumft, W.G.2    Kroneck, P.M.3
  • 25
    • 0035977617 scopus 로고    scopus 로고
    • Characterization of the copper-sulfur chromophores in nitrous oxide reductase by resonance Raman spectroscopy: Evidence for sulfur coordination in the catalytic cluster
    • (doi:10.1021/ja994322i)
    • Alvarez, M. L., Ai, J., Zumft, W., Sanders-Loehr, J. & Dooley, D. M. 2001 Characterization of the copper-sulfur chromophores in nitrous oxide reductase by resonance Raman spectroscopy: evidence for sulfur coordination in the catalytic cluster. J. Am. Chem. Soc. 123, 576-587. (doi:10.1021/ja994322i)
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 576-587
    • Alvarez, M.L.1    Ai, J.2    Zumft, W.3    Sanders-Loehr, J.4    Dooley, D.M.5
  • 26
    • 0025934978 scopus 로고
    • A model of the copper centres of nitrous oxide reductase (Pseudomonas stutzeri). Evidence from optical, EPR and MCD spectroscopy
    • (doi:10.1016/0014-5793(91) 81331-2)
    • Farrar, J. A., Thomson, A. J., Cheesman, M. R., Dooley, D. M. & Zumft, W. G. 1991 A model of the copper centres of nitrous oxide reductase (Pseudomonas stutzeri). Evidence from optical, EPR and MCD spectroscopy. FEBS Lett. 294, 11-15. (doi:10.1016/0014-5793(91) 81331-2)
    • (1991) FEBS Lett. , vol.294 , pp. 11-15
    • Farrar, J.A.1    Thomson, A.J.2    Cheesman, M.R.3    Dooley, D.M.4    Zumft, W.G.5
  • 27
    • 0032824420 scopus 로고    scopus 로고
    • A cytochrome c peroxidase from Pseudomonas nautica 617 active at high ionic strength: Expression, purification and characterization
    • (doi:10.1016/S0167-4838(99)00188-0)
    • Alves, T. et al. 1999 A cytochrome c peroxidase from Pseudomonas nautica 617 active at high ionic strength: expression, purification and characterization. Biochim. Biophys. Acta 1434, 248-259. (doi:10.1016/S0167-4838(99)00188-0)
    • (1999) Biochim. Biophys. Acta , vol.1434 , pp. 248-259
    • Alves, T.1
  • 28
    • 0002936816 scopus 로고
    • A study of spore formation and other morphological characteristics of Vibrio desulphuricans
    • (doi:10.1007/BF00407364)
    • Starkey, R. L. 1938 A study of spore formation and other morphological characteristics of Vibrio desulphuricans. Arch. Mikrobiol. 8, 268-304. (doi:10.1007/BF00407364)
    • (1938) Arch. Mikrobiol. , vol.8 , pp. 268-304
    • Starkey, R.L.1
  • 29
    • 0025211779 scopus 로고
    • Quantitation of protein
    • (doi:10.1016/0076-6879(90) 82008-P)
    • Stoscheck, C. 1990 Quantitation of protein. Methods Enzymol. 182, 50-68. (doi:10.1016/0076-6879(90) 82008-P)
    • (1990) Methods Enzymol. , vol.182 , pp. 50-68
    • Stoscheck, C.1
  • 30
    • 0001349923 scopus 로고
    • The determination of cuprous ion in copper proteins
    • (doi:10.1016/0003-9861(60)90168-5)
    • Felsenfeld, G. 1960 The determination of cuprous ion in copper proteins. Arch. Biochem. Biophys. 87, 247-251. (doi:10.1016/0003-9861(60)90168-5)
    • (1960) Arch. Biochem. Biophys. , vol.87 , pp. 247-251
    • Felsenfeld, G.1
  • 34
    • 4544231537 scopus 로고    scopus 로고
    • 2O reduction by the mu4-sulfide-bridged tetranuclear CuZ cluster active site
    • (doi:10.1002/anie.200301734)
    • 2O reduction by the mu4-sulfide-bridged tetranuclear CuZ cluster active site. Angew. Chem. Int. Ed. Engl. 43, 4132-4140. (doi:10.1002/anie.200301734)
    • (2004) Angew. Chem. Int. Ed. Engl. , vol.43 , pp. 4132-4140
    • Chen, P.1    Gorelsky, S.I.2    Ghosh, S.3    Solomon, E.I.4
  • 35
    • 2342640978 scopus 로고    scopus 로고
    • Characterisation of [Cu4S], the catalytic site in nitrous oxide reductase, by EPR spectroscopy
    • (doi:10.1039/b313913a)
    • Oganesyan, V. S., Rasmussen, T., Fairhurst, S. & Thomson, A. J. 2004 Characterisation of [Cu4S], the catalytic site in nitrous oxide reductase, by EPR spectroscopy. Dalton Trans. 7, 996-1002. (doi:10.1039/b313913a)
    • (2004) Dalton Trans. , vol.7 , pp. 996-1002
    • Oganesyan, V.S.1    Rasmussen, T.2    Fairhurst, S.3    Thomson, A.J.4
  • 37
    • 30744454598 scopus 로고    scopus 로고
    • 2O reduction by the mu4-S tetranuclear CuZ cluster of nitrous oxide reductase
    • (doi:10.1021/ja055856o)
    • 2O reduction by the mu4-S tetranuclear CuZ cluster of nitrous oxide reductase. J. Am. Chem. Soc. 128, 278-290. (doi:10.1021/ja055856o)
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 278-290
    • Gorelsky, S.I.1    Ghosh, S.2    Solomon, E.I.3
  • 38
    • 80052577976 scopus 로고    scopus 로고
    • N(2)O binding at a [4Cu:2S] copper-sulphur cluster in nitrous oxide reductase
    • (doi:10. 1038/nature10332)
    • Pomowski, A., Zumft, W., Kroneck, P. & Einsle, O. 2011 N(2)O binding at a [4Cu:2S] copper-sulphur cluster in nitrous oxide reductase. Nature 477, 234-237. (doi:10. 1038/nature10332)
    • (2011) Nature , vol.477 , pp. 234-237
    • Pomowski, A.1    Zumft, W.2    Kroneck, P.3    Einsle, O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.