메뉴 건너뛰기




Volumn 1837, Issue 3, 2014, Pages 375-384

Steady-state kinetics with nitric oxide reductase (NOR): New considerations on substrate inhibition profile and catalytic mechanism

Author keywords

Electrochemistry; Enzyme kinetics; NO reduction; NOR

Indexed keywords

GRAPHITE; NITRIC OXIDE REDUCTASE;

EID: 84892396381     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2014.01.001     Document Type: Article
Times cited : (27)

References (57)
  • 1
    • 0024961947 scopus 로고
    • Purification and some characteristics of nitric oxide reductase-containing vesicles from Paracoccus denitrificans
    • J. Hoglen, and T.C. Hollocher Purification and some characteristics of nitric oxide reductase-containing vesicles from Paracoccus denitrificans J. Biol. Chem. 264 1989 7556 7563
    • (1989) J. Biol. Chem. , vol.264 , pp. 7556-7563
    • Hoglen, J.1    Hollocher, T.C.2
  • 2
    • 0025309975 scopus 로고
    • The nitric oxide reductase of Paracoccus denitrificans
    • G.J. Carr, and S.J. Ferguson The nitric oxide reductase of Paracoccus denitrificans Biochem. J. 269 1990 423 429 (Pubitemid 20236034)
    • (1990) Biochemical Journal , vol.269 , Issue.2 , pp. 423-429
    • Carr, G.J.1    Ferguson, S.J.2
  • 3
    • 0024335650 scopus 로고
    • Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri
    • B. Heiss, K. Frunzke, and W.G. Zumft Formation of the NN bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri J. Bacteriol. 171 1989 3288 3297 (Pubitemid 19145684)
    • (1989) Journal of Bacteriology , vol.171 , Issue.6 , pp. 3288-3297
    • Heiss, B.1    Frunzke Zumft, K.W.G.2
  • 4
    • 0028306590 scopus 로고
    • Nitric oxide reductase from Pseudomonas stutzeri, a novel cytochrome bc complex. Phospholipid requirement, electron paramagnetic resonance and redox properties
    • DOI 10.1111/j.1432-1033.1994.tb18868.x
    • D.H. Kastrau, B. Heiss, P.M. Kroneck, and W.G. Zumft Nitric oxide reductase from Pseudomonas stutzeri, a novel cytochrome bc complex. Phospholipid requirement, electron paramagnetic resonance and redox properties Eur. J. Biochem. 222 1994 293 303 (Pubitemid 24204898)
    • (1994) European Journal of Biochemistry , vol.222 , Issue.2 , pp. 293-303
    • Kastrau, D.H.W.1    Heiss, B.2    Kroneck, P.M.H.3    Zumft, W.G.4
  • 5
    • 11244302439 scopus 로고    scopus 로고
    • NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: Characterization of reaction intermediates that appear in the single turnover cycle
    • DOI 10.1074/jbc.M409996200
    • H. Kumita, K. Matsuura, T. Hino, S. Takahashi, H. Hori, Y. Fukumori, I. Morishima, and Y. Shiro NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: characterization of reaction intermediates that appear in the single turnover cycle J. Biol. Chem. 279 2004 55247 55254 (Pubitemid 40066521)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55247-55254
    • Kumita, H.1    Matsuura, K.2    Hino, T.3    Takahashi, S.4    Hori, H.5    Fukumori, Y.6    Morishima, I.7    Shiro, Y.8
  • 7
    • 19544375814 scopus 로고
    • Marinobacter hydrocarbonoclasticus Gauthier, et al. 1992 and Marinobacter aquaeolei Nguyen et al. 1999 are heterotypic synonyms
    • M.C. Marquez, and A. Ventosa Marinobacter hydrocarbonoclasticus Gauthier, et al. 1992 and Marinobacter aquaeolei Nguyen et al. 1999 are heterotypic synonyms Int. J. Syst. Evol. Microbiol. 55 2005 1992 1349 1351
    • (1992) Int. J. Syst. Evol. Microbiol. , vol.55 , Issue.2005 , pp. 1349-1351
    • Marquez, M.C.1    Ventosa, A.2
  • 8
    • 10444275550 scopus 로고    scopus 로고
    • Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme-copper oxidase type
    • DOI 10.1016/j.jinorgbio.2004.09.024, PII S0162013404002909, Heme-Diatomic Interactions, Part 1
    • W.G. Zumft Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme-copper oxidase type J. Inorg. Biochem. 99 2005 194 215 (Pubitemid 39642979)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 194-215
    • Zumft, W.G.1
  • 9
    • 33750959735 scopus 로고    scopus 로고
    • Metalloenzymes of the denitrification pathway
    • DOI 10.1016/j.jinorgbio.2006.09.003, PII S0162013406002534
    • P. Tavares, A.S. Pereira, J.J. Moura, and I. Moura Metalloenzymes of the denitrification pathway J. Inorg. Biochem. 100 2006 2087 2100 (Pubitemid 44738047)
    • (2006) Journal of Inorganic Biochemistry , vol.100 , Issue.12 , pp. 2087-2100
    • Tavares, P.1    Pereira, A.S.2    Moura, J.J.G.3    Moura, I.4
  • 11
    • 0031028099 scopus 로고    scopus 로고
    • Purification and initial kinetic and spectroscopic characterization of NO reductase from Paracoccus denitrificans
    • DOI 10.1016/S0005-2728(96)00138-7, PII S0005272896001387
    • P. Girsch, and S. de Vries Purification and initial kinetic and spectroscopic characterization of NO reductase from Paracoccus denitrificans Biochim. Biophys. Acta 1318 1997 202 216 (Pubitemid 27051234)
    • (1997) Biochimica et Biophysica Acta - Bioenergetics , vol.1318 , Issue.1-2 , pp. 202-216
    • Girsch, P.1    De Vries, S.2
  • 12
    • 0032558389 scopus 로고    scopus 로고
    • The active site of the bacterial nitric oxide reductase is a dinuclear iron center
    • DOI 10.1021/bi980943x
    • J. Hendriks, A. Warne, U. Gohlke, T. Haltia, C. Ludovici, M. Lubben, and M. Saraste The active site of the bacterial nitric oxide reductase is a dinuclear iron center Biochemistry 37 1998 13102 13109 (Pubitemid 28449553)
    • (1998) Biochemistry , vol.37 , Issue.38 , pp. 13102-13109
    • Hendriks, J.1    Warne, A.2    Gohlke, U.3    Haltia, T.4    Ludovici, C.5    Lubben, M.6    Saraste, M.7
  • 13
    • 0032539983 scopus 로고    scopus 로고
    • The MCD and EPR of the heme centers of nitric oxide reductase from Pseudomonas stutzeri: Evidence that the enzyme is structurally related to the heme-copper oxidases
    • DOI 10.1021/bi972437y
    • M.R. Cheesman, W.G. Zumft, and A.J. Thomson The MCD and EPR of the heme centers of nitric oxide reductase from Pseudomonas stutzeri: evidence that the enzyme is structurally related to the heme-copper oxidases Biochemistry 37 1998 3994 4000 (Pubitemid 28162957)
    • (1998) Biochemistry , vol.37 , Issue.11 , pp. 3994-4000
    • Cheesman, M.R.1    Zumft, W.G.2    Thomson, A.J.3
  • 15
    • 78650307247 scopus 로고    scopus 로고
    • Structural basis of biological N2O generation by bacterial nitric oxide reductase
    • (New York, N.Y.)
    • T. Hino, Y. Matsumoto, S. Nagano, H. Sugimoto, Y. Fukumori, T. Murata, S. Iwata, and Y. Shiro Structural basis of biological N2O generation by bacterial nitric oxide reductase Science 330 2010 1666 1670 (New York, N.Y.)
    • (2010) Science , vol.330 , pp. 1666-1670
    • Hino, T.1    Matsumoto, Y.2    Nagano, S.3    Sugimoto, H.4    Fukumori, Y.5    Murata, T.6    Iwata, S.7    Shiro, Y.8
  • 17
    • 0029988772 scopus 로고    scopus 로고
    • Cytochrome cb-type nitric oxide reductase with cytochrome c oxidase activity from Paracoccus denitrificans ATCC 35512
    • T. Fujiwara, and Y. Fukumori Cytochrome cb-type nitric oxide reductase with cytochrome c oxidase activity from Paracoccus denitrificans ATCC 35512 J. Bacteriol. 178 1996 1866 1871 (Pubitemid 26110528)
    • (1996) Journal of Bacteriology , vol.178 , Issue.7 , pp. 1866-1871
    • Fujiwara, T.1    Fukumori, Y.2
  • 18
    • 0030694779 scopus 로고    scopus 로고
    • Isolation and characterization of nitric oxide reductase from Paracoccus halodenitrificans
    • DOI 10.1021/bi971070u
    • N. Sakurai, and T. Sakurai Isolation and characterization of nitric oxide reductase from Paracoccus halodenitrificans Biochemistry 36 1997 13809 13815 (Pubitemid 27494886)
    • (1997) Biochemistry , vol.36 , Issue.45 , pp. 13809-13815
    • Sakurai, N.1    Sakurai, T.2
  • 19
    • 23244445035 scopus 로고    scopus 로고
    • Electron/proton coupling in bacterial nitric oxide reductase during reduction of oxygen
    • DOI 10.1021/bi050524h
    • U. Flock, N.J. Watmough, and P. Adelroth Electron/proton coupling in bacterial nitric oxide reductase during reduction of oxygen Biochemistry 44 2005 10711 10719 (Pubitemid 41098248)
    • (2005) Biochemistry , vol.44 , Issue.31 , pp. 10711-10719
    • Flock, U.1    Watmough, N.J.2    Adelroth, P.3
  • 20
    • 33845397190 scopus 로고    scopus 로고
    • Nitric oxide reductase: Direct electrochemistry and electrocatalytic activity
    • DOI 10.1002/cbic.200600253
    • C.M. Cordas, A.S. Pereira, C.E. Martins, C.G. Timoteo, I. Moura, J.J. Moura, and P. Tavares Nitric oxide reductase: direct electrochemistry and electrocatalytic activity Chembiochem 7 2006 1878 1881 (Pubitemid 44893519)
    • (2006) ChemBioChem , vol.7 , Issue.12 , pp. 1878-1881
    • Cordas, C.M.1    Pereira, A.S.2    Martins, C.E.3    Timoteo, C.G.4    Moura, I.5    Moura, J.J.G.6    Tavares, P.7
  • 21
    • 64449084988 scopus 로고    scopus 로고
    • Exploring the terminal region of the proton pathway in the bacterial nitric oxide reductase
    • U. Flock, P. Lachmann, J. Reimann, N.J. Watmough, and P. Adelroth Exploring the terminal region of the proton pathway in the bacterial nitric oxide reductase J. Inorg. Biochem. 103 2009 845 850
    • (2009) J. Inorg. Biochem. , vol.103 , pp. 845-850
    • Flock, U.1    Lachmann, P.2    Reimann, J.3    Watmough, N.J.4    Adelroth, P.5
  • 22
    • 34247472629 scopus 로고    scopus 로고
    • A pathway for protons in nitric oxide reductase from Paracoccus denitrificans
    • DOI 10.1016/j.bbabio.2007.03.006, PII S0005272807000680
    • J. Reimann, U. Flock, H. Lepp, A. Honigmann, and P. Adelroth A pathway for protons in nitric oxide reductase from Paracoccus denitrificans Biochim. Biophys. Acta 1767 2007 362 373 (Pubitemid 46659879)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.5 , pp. 362-373
    • Reimann, J.1    Flock, U.2    Lepp, H.3    Honigmann, A.4    Adelroth, P.5
  • 23
    • 34249789578 scopus 로고    scopus 로고
    • Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins
    • DOI 10.1039/b604194a
    • P. Moenne-Loccoz Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins Nat. Prod. Rep. 24 2007 610 620 (Pubitemid 46848713)
    • (2007) Natural Product Reports , vol.24 , Issue.3 , pp. 610-620
    • Moenne-Loccoz, P.1
  • 25
    • 84870393902 scopus 로고    scopus 로고
    • Mono- and dinuclear non-heme iron-nitrosyl complexes: Models for key intermediates in bacterial nitric oxide reductases
    • T. Berto, A.L. Speelman, S. Zheng, and N. Lehnert Mono- and dinuclear non-heme iron-nitrosyl complexes: models for key intermediates in bacterial nitric oxide reductases Coord. Chem. Rev. 257 2012 255 259
    • (2012) Coord. Chem. Rev. , vol.257 , pp. 255-259
    • Berto, T.1    Speelman, A.L.2    Zheng, S.3    Lehnert, N.4
  • 26
    • 84875762801 scopus 로고    scopus 로고
    • The functional model complex [Fe(BPMP)(OPr)(NO)](BPh) provides insight into the mechanism of flavodiiron NO reductases
    • S. Zheng, T.C. Berto, E.W. Dahl, M.B. Hoffman, A.L. Speelman, and N. Lehnert The functional model complex [Fe(BPMP)(OPr)(NO)](BPh) provides insight into the mechanism of flavodiiron NO reductases J. Am. Chem. Soc. 135 2013 4902 4905
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 4902-4905
    • Zheng, S.1    Berto, T.C.2    Dahl, E.W.3    Hoffman, M.B.4    Speelman, A.L.5    Lehnert, N.6
  • 27
    • 0342894038 scopus 로고    scopus 로고
    • A low-redox potential heme in the dinuclear center of bacterial nitric oxide reductase: Implications for the evolution of energy-conserving heme- copper oxidases
    • DOI 10.1021/bi9916426
    • K.L. Gronberg, M.D. Roldan, L. Prior, G. Butland, M.R. Cheesman, D.J. Richardson, S. Spiro, A.J. Thomson, and N.J. Watmough A low-redox potential heme in the dinuclear center of bacterial nitric oxide reductase: implications for the evolution of energy-conserving heme-copper oxidases Biochemistry 38 1999 13780 13786 (Pubitemid 29504207)
    • (1999) Biochemistry , vol.38 , Issue.42 , pp. 13780-13786
    • Gronberg, K.L.C.1    Roldan, M.D.2    Prior, L.3    Butland, G.4    Cheesman, M.R.5    Richardson, D.J.6    Spiro, S.7    Thomson, A.J.8    Watmough, N.J.9
  • 28
    • 84862888168 scopus 로고    scopus 로고
    • Mechanism for N(2)O generation in bacterial nitric oxide reductase: A quantum chemical study
    • M.R. Blomberg, and P.E. Siegbahn Mechanism for N(2)O generation in bacterial nitric oxide reductase: a quantum chemical study Biochemistry 51 2012 5173 5186
    • (2012) Biochemistry , vol.51 , pp. 5173-5186
    • Blomberg, M.R.1    Siegbahn, P.E.2
  • 29
    • 0141777543 scopus 로고    scopus 로고
    • Structural characterization of the catalytic high-spin heme b of nitric oxide reductase: A resonance Raman study
    • DOI 10.1021/ja973671e
    • P. Moenne-Loccoz, and S. de Vries Structural characterization of the catalytic high-spin heme b of nitric oxide reductase: a resonance Raman study J. Am. Chem. Soc. 120 1998 5147 5152 (Pubitemid 28328876)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.21 , pp. 5147-5152
    • Moenne-Loccoz, P.1    De Vries, S.2
  • 30
    • 0037133132 scopus 로고    scopus 로고
    • Proton and electron pathways in the bacterial nitric oxide reductase
    • DOI 10.1021/bi0121050
    • J.H. Hendriks, A. Jasaitis, M. Saraste, and M.I. Verkhovsky Proton and electron pathways in the bacterial nitric oxide reductase Biochemistry 41 2002 2331 2340 (Pubitemid 34160895)
    • (2002) Biochemistry , vol.41 , Issue.7 , pp. 2331-2340
    • Hendriks, J.H.M.1    Jasaitis, A.2    Saraste, M.3    Verkhovsky, M.I.4
  • 31
    • 84857911507 scopus 로고    scopus 로고
    • Molecular structure and function of bacterial nitric oxide reductase
    • T. Hino, S. Nagano, H. Sugimoto, T. Tosha, and Y. Shiro Molecular structure and function of bacterial nitric oxide reductase Biochim. Biophys. Acta 1817 2011 680 687
    • (2011) Biochim. Biophys. Acta , vol.1817 , pp. 680-687
    • Hino, T.1    Nagano, S.2    Sugimoto, H.3    Tosha, T.4    Shiro, Y.5
  • 32
    • 57549100205 scopus 로고    scopus 로고
    • Intermediates involved in the two electron reduction of NO to N2O by a functional synthetic model of heme containing bacterial NO reductase
    • J.P. Collman, A. Dey, Y. Yang, R.A. Decreau, T. Ohta, and E.I. Solomon Intermediates involved in the two electron reduction of NO to N2O by a functional synthetic model of heme containing bacterial NO reductase J. Am. Chem. Soc. 130 2008 16498 16499
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 16498-16499
    • Collman, J.P.1    Dey, A.2    Yang, Y.3    Decreau, R.A.4    Ohta, T.5    Solomon, E.I.6
  • 34
    • 77952700938 scopus 로고    scopus 로고
    • Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin
    • Y.W. Lin, N. Yeung, Y.G. Gao, K.D. Miner, S. Tian, H. Robinson, and Y. Lu Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin Proc. Natl. Acad. Sci. U. S. A. 107 2010 8581 8586
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 8581-8586
    • Lin, Y.W.1    Yeung, N.2    Gao, Y.G.3    Miner, K.D.4    Tian, S.5    Robinson, H.6    Lu, Y.7
  • 35
    • 79959808611 scopus 로고    scopus 로고
    • Spectroscopic characterization of mononitrosyl complexes in heme-nonheme diiron centers within the myoglobin scaffold (Fe(B)Mbs): Relevance to denitrifying NO reductase
    • T. Hayashi, K.D. Miner, N. Yeung, Y.W. Lin, Y. Lu, and P. Moenne-Loccoz Spectroscopic characterization of mononitrosyl complexes in heme-nonheme diiron centers within the myoglobin scaffold (Fe(B)Mbs): relevance to denitrifying NO reductase Biochemistry 50 2011 5939 5947
    • (2011) Biochemistry , vol.50 , pp. 5939-5947
    • Hayashi, T.1    Miner, K.D.2    Yeung, N.3    Lin, Y.W.4    Lu, Y.5    Moenne-Loccoz, P.6
  • 37
    • 84871853154 scopus 로고    scopus 로고
    • Electrochemical behaviour of bacterial nitric oxide reductase-evidence of low redox potential non-heme Fe(B) gives new perspectives on the catalytic mechanism
    • C.M. Cordas, A.G. Duarte, J.J. Moura, and I. Moura Electrochemical behaviour of bacterial nitric oxide reductase-evidence of low redox potential non-heme Fe(B) gives new perspectives on the catalytic mechanism Biochim. Biophys. Acta 1827 2013 233 238
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 233-238
    • Cordas, C.M.1    Duarte, A.G.2    Moura, J.J.3    Moura, I.4
  • 38
    • 0345363246 scopus 로고    scopus 로고
    • Kinetic analysis of substrate inhibition in nitric oxide reductase of Paracoccus denitrificans
    • DOI 10.1006/bbrc.1999.1245
    • M. Koutny, and I. Kucera Kinetic analysis of substrate inhibition in nitric oxide reductase of Paracoccus denitrificans Biochem. Biophys. Res. Commun. 262 1999 562 564 (Pubitemid 29429907)
    • (1999) Biochemical and Biophysical Research Communications , vol.262 , Issue.2 , pp. 562-564
    • Koutny, M.1    Kucera, I.2
  • 39
    • 77955498374 scopus 로고    scopus 로고
    • Substrate control of internal electron transfer in bacterial nitric-oxide reductase
    • P. Lachmann, Y. Huang, J. Reimann, U. Flock, and P. Adelroth Substrate control of internal electron transfer in bacterial nitric-oxide reductase J. Biol. Chem. 285 2010 25531 25537
    • (2010) J. Biol. Chem. , vol.285 , pp. 25531-25537
    • Lachmann, P.1    Huang, Y.2    Reimann, J.3    Flock, U.4    Adelroth, P.5
  • 41
    • 0000481224 scopus 로고
    • Caractérisation préliminaire de système cytochromique de la bactérie marine dénitrifiante Pseudomonas nautica 617
    • G. Fauque, J.J.G.S. Besson, L. Saraiva, and I. Moura Caracté risation préliminaire de système cytochromique de la bactérie marine dénitrifiante Pseudomonas nautica 617 Oceans 18 1992 211 216
    • (1992) Oceans , vol.18 , pp. 211-216
    • Fauque, G.1    Besson, J.J.G.S.2    Saraiva, L.3    Moura, I.4
  • 43
    • 0034691286 scopus 로고    scopus 로고
    • 4-type cytochrome isolated from Thiobacillus ferrooxidans
    • DOI 10.1021/bi992846p
    • M.T. Giudici-Orticoni, G. Leroy, W. Nitschke, and M. Bruschi Characterization of a new dihemic c(4)-type cytochrome isolated from Thiobacillus ferrooxidans Biochemistry 39 2000 7205 7211 (Pubitemid 30413110)
    • (2000) Biochemistry , vol.39 , Issue.24 , pp. 7205-7211
    • Giudici-Orticoni, M.-T.1    Leroy, G.2    Nitschke, W.3    Bruschi, M.4
  • 44
    • 0028291355 scopus 로고
    • Characterization of the dihemic cytochrome c549 from the marine denitrifying bacterium Pseudomonas nautica 617
    • L.M. Saraiva, S. Besson, G. Fauque, and I. Moura Characterization of the dihemic cytochrome c549 from the marine denitrifying bacterium Pseudomonas nautica 617 Biochem. Biophys. Res. Commun. 199 1994 1289 1296
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 1289-1296
    • Saraiva, L.M.1    Besson, S.2    Fauque, G.3    Moura, I.4
  • 45
    • 0029088401 scopus 로고
    • Purification and preliminary characterization of three c-type cytochromes from Pseudomonas nautica strain 617
    • L.M. Saraiva, S. Besson, I. Moura, and G. Fauque Purification and preliminary characterization of three c-type cytochromes from Pseudomonas nautica strain 617 Biochem. Biophys. Res. Commun. 212 1995 1088 1097
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 1088-1097
    • Saraiva, L.M.1    Besson, S.2    Moura, I.3    Fauque, G.4
  • 46
    • 0028050131 scopus 로고
    • 552 from Pseudomonas nautica 617
    • L.M. Saraiva, G. Fauque, S. Besson, and I. Moura Physico-chemical and spectroscopic properties of the monohemic cytochrome C552 from Pseudomonas nautica 617 Eur. J. Biochem. 224 1994 1011 1017 (Pubitemid 24288865)
    • (1994) European Journal of Biochemistry , vol.224 , Issue.3 , pp. 1011-1017
    • Saraiva, L.M.1    Fauque, G.2    Besson, S.3    Moura, I.4
  • 49
    • 49049115593 scopus 로고    scopus 로고
    • Direct electrochemistry of redox enzymes as a tool for mechanistic studies
    • C. Leger, and P. Bertrand Direct electrochemistry of redox enzymes as a tool for mechanistic studies Chem. Rev. 108 2008 2379 2438
    • (2008) Chem. Rev. , vol.108 , pp. 2379-2438
    • Leger, C.1    Bertrand, P.2
  • 50
    • 80055008008 scopus 로고    scopus 로고
    • Structural and electronic characterization of non-heme Fe(II)-nitrosyls as biomimetic models of the FeB Center of Bacterial Nitric Oxide Reductase (NorBC)
    • T.C. Berto, M.B. Hoffman, Y. Murata, K.B. Landenberger, E.E. Alp, J. Zhao, and N. Lehnert Structural and electronic characterization of non-heme Fe(II)-nitrosyls as biomimetic models of the FeB Center of Bacterial Nitric Oxide Reductase (NorBC) J. Am. Chem. Soc. 133 2011 16714 16717
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 16714-16717
    • Berto, T.C.1    Hoffman, M.B.2    Murata, Y.3    Landenberger, K.B.4    Alp, E.E.5    Zhao, J.6    Lehnert, N.7
  • 52
    • 77955454905 scopus 로고    scopus 로고
    • Electronic structure of heme-nitrosyls and its significance for nitric oxide reactivity, sensing, transport, and toxicity in biological systems
    • L.E. Goodrich, F. Paulat, V.K. Praneeth, and N. Lehnert Electronic structure of heme-nitrosyls and its significance for nitric oxide reactivity, sensing, transport, and toxicity in biological systems Inorg. Chem. 49 2010 6293 6316
    • (2010) Inorg. Chem. , vol.49 , pp. 6293-6316
    • Goodrich, L.E.1    Paulat, F.2    Praneeth, V.K.3    Lehnert, N.4
  • 53
    • 68949211401 scopus 로고    scopus 로고
    • Dinitrosyl iron complexes (DNICs) bearing O-bound nitrito ligand: Reversible transformation between the six-coordinate {Fe(NO)2}9 [(1-MeIm)2(eta(2)-ONO)Fe(NO)2] (g = 2.013) and four-coordinate {Fe(NO)2}9 [(1-MeIm)(ONO)Fe(NO)2] (g = 2.03)
    • F.T. Tsai, T.S. Kuo, and W.F. Liaw Dinitrosyl iron complexes (DNICs) bearing O-bound nitrito ligand: reversible transformation between the six-coordinate {Fe(NO)2}9 [(1-MeIm)2(eta(2)-ONO)Fe(NO)2] (g = 2.013) and four-coordinate {Fe(NO)2}9 [(1-MeIm)(ONO)Fe(NO)2] (g = 2.03) J. Am. Chem. Soc. 131 2009 3426 3427
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3426-3427
    • Tsai, F.T.1    Kuo, T.S.2    Liaw, W.F.3
  • 54
    • 35548960532 scopus 로고    scopus 로고
    • EPR, UV-vis, IR, and X-ray demonstration of the anionic dimeric dinitrosyl iron complex [(NO)(2)Fe(micro-S(t)Bu)(2)Fe(NO)(2)](-): Relevance to the products of nitrosylation of cytosolic and mitochondrial aconitases, and high-potential iron proteins
    • C.C. Tsou, T.T. Lu, and W.F. Liaw EPR, UV-vis, IR, and X-ray demonstration of the anionic dimeric dinitrosyl iron complex [(NO)(2)Fe(micro-S(t)Bu)(2)Fe(NO)(2)](-): relevance to the products of nitrosylation of cytosolic and mitochondrial aconitases, and high-potential iron proteins J. Am. Chem. Soc. 129 2007 12626 12627
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 12626-12627
    • Tsou, C.C.1    Lu, T.T.2    Liaw, W.F.3
  • 55
    • 34548775168 scopus 로고    scopus 로고
    • Flavo-diiron enzymes: Nitric oxide or dioxygen reductases?
    • J.D.M. Kurtz Flavo-diiron enzymes: nitric oxide or dioxygen reductases? Dalton Trans. 2007 4115 4121
    • (2007) Dalton Trans. , pp. 4115-4121
    • Kurtz, J.D.M.1
  • 57
    • 77955812490 scopus 로고    scopus 로고
    • Introducing a 2-His-1-Glu nonheme iron center into myoglobin confers nitric oxide reductase activity
    • Y.W. Lin, N. Yeung, Y.G. Gao, K.D. Miner, L. Lei, H. Robinson, and Y. Lu Introducing a 2-His-1-Glu nonheme iron center into myoglobin confers nitric oxide reductase activity J. Am. Chem. Soc. 132 2010 9970 9972
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9970-9972
    • Lin, Y.W.1    Yeung, N.2    Gao, Y.G.3    Miner, K.D.4    Lei, L.5    Robinson, H.6    Lu, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.