메뉴 건너뛰기




Volumn 51, Issue 25, 2012, Pages 5173-5186

Mechanism for N2O generation in bacterial nitric oxide reductase: A quantum chemical study

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ANTIFERRO-MAGNETICALLY COUPLED; BACTERIAL ENZYMES; BINUCLEAR CENTER; CATALYTIC CYCLES; CATALYTIC MECHANISMS; EXPERIMENTAL OBSERVATION; FERRIC IRON; HYBRID DENSITY FUNCTIONAL THEORY; NITRIC OXIDE REDUCTASE; NO CONCENTRATION; OXIDIZED ENZYME; PH-DEPENDENT; QUANTUM CHEMICAL STUDIES; SUBSTRATE INHIBITION;

EID: 84862888168     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300496e     Document Type: Article
Times cited : (79)

References (41)
  • 1
    • 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
    • Girsch, P. and de Vries, S. (1997) Purification and initial kinetic and spectroscopic characterization of NO reductase from Paracoccus denitrificans Biochim. Biophys. Acta 1318, 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
  • 2
    • 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
    • Moënne-Loccoz, P. and de Vries, S. (1998) Structural Characterization of the Catalytic High-Spin Heme b of Nitric Oxide Reductase: A Resonance Raman Study J. Am. Chem. Soc. 120, 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
  • 7
    • 33745203021 scopus 로고    scopus 로고
    • Reduction of Nitric Oxide in Bacterial Nitric Oxide Reductase: A Theoretical Model Study
    • Blomberg, L. M., Blomberg, M. R. A., and Siegbahn, P. E. M. (2006) Reduction of Nitric Oxide in Bacterial Nitric Oxide Reductase: A Theoretical Model Study Biochim. Biophys. Acta 1757, 240-252
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 240-252
    • Blomberg, L.M.1    Blomberg, M.R.A.2    Siegbahn, P.E.M.3
  • 8
    • 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
    • Moënne-Loccoz, P. (2007) Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins Nat. Prod. Rep. 24, 610-620 (Pubitemid 46848713)
    • (2007) Natural Product Reports , vol.24 , Issue.3 , pp. 610-620
    • Moenne-Loccoz, P.1
  • 11
    • 0021931295 scopus 로고
    • Nitric oxide-dependent proton translocation in various denitrifiers
    • Shapleigh, J. P. and Payne, W. J. (1985) Nitric oxide-dependent proton translocation in various denitrifiers J. Bacteriol. 163, 837-840 (Pubitemid 15230710)
    • (1985) Journal of Bacteriology , vol.163 , Issue.3 , pp. 837-840
    • Shapleigh, J.P.1    Payne, W.J.2
  • 12
    • 0037133132 scopus 로고    scopus 로고
    • Proton and electron pathways in the bacterial nitric oxide reductase
    • DOI 10.1021/bi0121050
    • Hendriks, J. H., Jasitis, A., Saraste, M., and Verkhovski, M. I. (2002) Proton and electron pathways in the bacterial nitric oxide reductase Biochemistry 41, 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
  • 13
    • 84857911507 scopus 로고    scopus 로고
    • Molecular structure and function of bacterial nitric oxide reductase
    • Hino, T., Nagano, S., Sugimoto, H., Tosha, T., and Shiro, Y. (2012) Molecular structure and function of bacterial nitric oxide reductase Biochim. Biophys. Acta 1817, 680-687
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 680-687
    • Hino, T.1    Nagano, S.2    Sugimoto, H.3    Tosha, T.4    Shiro, Y.5
  • 14
    • 0037189501 scopus 로고    scopus 로고
    • Nitric-oxide reductase: Structure and properties of the catalytic site from resonance Raman scattering
    • DOI 10.1074/jbc.M201913200
    • Pinakoulaki, E., Gemeinhardt, S., Saraste, M., and Varotsis, C. (2002) Nitric-oxide Reductase, Structure and Properties of the catalytic site from resonance raman scattering J. Biol. Chem. 277, 23407-23413 (Pubitemid 34952172)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23407-23413
    • Pinakoulaki, E.1    Gemeinhardt, S.2    Saraste, M.3    Varotsis, C.4
  • 15
    • 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
    • Grönberg, K. L. C., Roldan, M. D., Prior, L., Butland, G., Cheessman, M. R., Richardson, D. J., Spiro, S., Thomson, A. J., and Watmough, N. J. (1999) 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, 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
  • 17
    • 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
    • Reimann, J., Flock, U., Lepp, H., Honigmann, A., and Ädelroth, P. (2007) A pathway for protons in nitric oxide reductase from Paracoccus denitrificans Biochim. Biophys. Acta 1767, 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
  • 18
    • 64449084988 scopus 로고    scopus 로고
    • Exploring the terminal region of the proton pathway in the bacterial nitric oxide reductase
    • Flock, U., Lachmann, P., Reimann, J., Watmough, N. J., and Ädelroth, P. (2009) Exploring the terminal region of the proton pathway in the bacterial nitric oxide reductase J. Inorg. Biochem. 103, 845-850
    • (2009) J. Inorg. Biochem. , vol.103 , pp. 845-850
    • Flock, U.1    Lachmann, P.2    Reimann, J.3    Watmough, N.J.4    Ädelroth, P.5
  • 19
    • 77955498374 scopus 로고    scopus 로고
    • Substrate control of internal electron transfer in bacterial nitric oxide reductase
    • Lachmann, P., Huang, Y., Reimann, J., Flock, U., and Ädelroth, P. (2010) Substrate control of internal electron transfer in bacterial nitric oxide reductase J. Biol. Chem. 285, 25531-25537
    • (2010) J. Biol. Chem. , vol.285 , pp. 25531-25537
    • Lachmann, P.1    Huang, Y.2    Reimann, J.3    Flock, U.4    Ädelroth, P.5
  • 20
    • 0035190144 scopus 로고    scopus 로고
    • Two conserved glutamates in the bacterial nitric oxide reductase are essential for activity but not assembly of the enzyme
    • DOI 10.1128/JB.183.1.189-199.2001
    • Butland, G., Spiro, S., Watmough, N. J., and Richardson, D. J. (2001) Two conserved glutamates in the bacterial nitric oxide reductase are essential for activity but not assembly of the enzyme J. Bacteriol. 183, 189-199 (Pubitemid 32003123)
    • (2001) Journal of Bacteriology , vol.183 , Issue.1 , pp. 189-199
    • Butland, G.1    Spiro, S.2    Watmough, N.J.3    Richardson, D.J.4
  • 21
    • 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
    • Zumft, W. G. (2005) Nitric oxide reductase of prokaryotes with emphasis on the respiratory heme-copper oxidase type J. Inorg. Biochem. 99, 194-215 (Pubitemid 39642979)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 194-215
    • Zumft, W.G.1
  • 22
    • 32544433641 scopus 로고
    • Density-Functional Theory of Spin Polarization and Spin Coupling in Iron-Sulfur Clusters
    • Noodleman, L. and Case, D. A. (1992) Density-Functional Theory of Spin Polarization and Spin Coupling in Iron-Sulfur Clusters Adv. Inorg. Chem. 38, 423-470
    • (1992) Adv. Inorg. Chem. , vol.38 , pp. 423-470
    • Noodleman, L.1    Case, D.A.2
  • 23
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • Becke, A. D. (1993) Density-functional thermochemistry. III. The role of exact exchange J. Chem. Phys. 98, 5648-5652
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 24
    • 0035730848 scopus 로고    scopus 로고
    • Reparameterization of hybrid functionals based on energy differences of states of different multiplicity
    • DOI 10.1007/s00214-001-0300-3
    • Reiher, M., Salomon, O., and Hess, B. A. (2001) Reparameterization of hybrid functionals based on energy differences of states of different multiplicity Theor. Chem. Acc. 107, 48-55 (Pubitemid 33576519)
    • (2001) Theoretical Chemistry Accounts , vol.107 , Issue.1 , pp. 48-55
    • Reiher, M.1    Salomon, O.2    Hess, B.A.3
  • 25
    • 84873407812 scopus 로고    scopus 로고
    • version 7.6 () Schrödinger, LLC, New York.
    • Jaguar, version 7.6 (2009) Schrödinger, LLC, New York.
    • (2009) Jaguar
  • 26
    • 34848916065 scopus 로고    scopus 로고
    • Double-hybrid density functionals with long-range dispersion corrections: Higher accuracy and extended applicability
    • Schwabe, T. and Grimme, S. (2007) Double-hybrid density functionals with long-range dispersion corrections: Higher accuracy and extended applicability Phys. Chem. Chem. Phys. 9, 3397-3406
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 3397-3406
    • Schwabe, T.1    Grimme, S.2
  • 27
    • 77956632873 scopus 로고    scopus 로고
    • Significant van der Waals Effects in Transition Metal Complexes
    • Siegbahn, P. E. M., Blomberg, M. R. A., and Chen, S.-L. (2010) Significant van der Waals Effects in Transition Metal Complexes J. Chem. Theory Comput. 6, 2040-2044
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 2040-2044
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2    Chen, S.-L.3
  • 28
    • 84961976154 scopus 로고    scopus 로고
    • Modeling electron transfer in biochemistry: A quantum chemical study of charge separation in Rhodobacter sphaeroides and photosystem II
    • DOI 10.1021/ja9805268
    • Blomberg, M. R. A., Siegbahn, P. E. M., and Babcock, G. T. (1998) Modeling electron transfer in biochemistry: A quantum chemical study of charge separation in Rhodobacter sphaeroides and photosystem II J. Am. Chem. Soc. 120, 8812-8824 (Pubitemid 28442920)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.34 , pp. 8812-8824
    • Blomberg, M.R.A.1    Siegbahn, P.E.M.2    Babcock, G.T.3
  • 29
    • 0001213712 scopus 로고    scopus 로고
    • Assessment of Gaussian-3 and density functional theories for a larger experimental test set
    • Curtiss, L. A., Raghavachari, K., Redfern, R. C., and Pople, J. A. (2000) Assessment of Gaussian-3 and density functional theories for a larger experimental test set J. Chem. Phys. 112, 7374-83
    • (2000) J. Chem. Phys. , vol.112 , pp. 7374-7383
    • Curtiss, L.A.1    Raghavachari, K.2    Redfern, R.C.3    Pople, J.A.4
  • 30
    • 0001181339 scopus 로고    scopus 로고
    • Density functional theory of biologically relevant metal centers
    • Siegbahn, P. E. M. and Blomberg, M. R. A. (1999) Density Functional Theory of Biologically Relevant Metal Centers Annu. Rev. Phys. Chem. 50, 221-249 (Pubitemid 129565549)
    • (1999) Annual Review of Physical Chemistry , vol.50 , pp. 221-249
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2
  • 31
    • 0038626673 scopus 로고    scopus 로고
    • revision B.03 () Gaussian Inc. Pittsburgh, PA.
    • Gaussian 03, revision B.03 (2003) Gaussian Inc., Pittsburgh, PA.
    • (2003) Gaussian 03
  • 32
    • 0142091718 scopus 로고    scopus 로고
    • A Theoretical Study of the Energetics of Proton Pumping and Oxygen Reduction in Cytochrome Oxidase
    • Siegbahn, P. E. M., Blomberg, M. R. A., and Blomberg, M. L. (2003) A Theoretical Study of the Energetics of Proton Pumping and Oxygen Reduction in Cytochrome Oxidase J. Phys. Chem. B 107, 10946-10955
    • (2003) J. Phys. Chem. B , vol.107 , pp. 10946-10955
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2    Blomberg, M.L.3
  • 33
    • 33746181702 scopus 로고    scopus 로고
    • Quantum chemistry applied to the mechanisms of transition metal containing enzymes - Cytochrome c oxidase, a particularly challenging case
    • DOI 10.1002/jcc.20448
    • Blomberg, M. R. A. and Siegbahn, P. E. M. (2006) Quantum Chemistry Applied to the Mechanisms of Transition Metal Containing Enzymes: Cytochrome c Oxidase a Particularly Challenging Case J. Comput. Chem. 27, 1373-1384 (Pubitemid 44230426)
    • (2006) Journal of Computational Chemistry , vol.27 , Issue.12 , pp. 1373-1384
    • Blomberg, M.R.A.1    Siegbahn, P.E.M.2
  • 34
    • 84889766662 scopus 로고    scopus 로고
    • Modeling of Mechanisms for Metalloenzymes Where Protons and Electrons Enter or Leave
    • In (Morokuma, K. and and Musaev, J. Eds.) pp, Wiley-VCH, Weinheim, Germany.
    • Siegbahn, P. E. M. and Blomberg, M. R. A. (2008) Modeling of Mechanisms for Metalloenzymes Where Protons and Electrons Enter or Leave. In Computational Modeling for Homogeneous Catalysis and Biocatalysis (Morokuma, K., and and Musaev, J., Eds.) pp 57-81, Wiley-VCH, Weinheim, Germany.
    • (2008) Computational Modeling for Homogeneous Catalysis and Biocatalysis , pp. 57-81
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2
  • 35
    • 78650084194 scopus 로고    scopus 로고
    • Quantum chemical studies of proton-coupled electron transfer in metalloenzymes
    • Siegbahn, P. E. M. and Blomberg, M. R. A. (2010) Quantum chemical studies of proton-coupled electron transfer in metalloenzymes Chem. Rev. 110, 7040-7061
    • (2010) Chem. Rev. , vol.110 , pp. 7040-7061
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2
  • 38
    • 68149092609 scopus 로고    scopus 로고
    • The Combined Picture from Theory and Experiments on Water Oxidation, Oxygen Reduction and Proton Pumping
    • Siegbahn, P. E. M. and Blomberg, M. R. A. (2009) The Combined Picture from Theory and Experiments on Water Oxidation, Oxygen Reduction and Proton Pumping Dalton Trans., 5832-5840
    • (2009) Dalton Trans. , pp. 5832-5840
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2
  • 39
  • 41
    • 84857922100 scopus 로고    scopus 로고
    • Cytochrome c oxidase and nitric oxide in action: Molecular mechanisms and pathophysiological implications
    • Sarti, P., Forte, E., Mastronicola, D., Guffre, A., and Arese, M. (2012) Cytochrome c oxidase and nitric oxide in action: Molecular mechanisms and pathophysiological implications Biochim. Biophys. Acta 1817, 610-619
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 610-619
    • Sarti, P.1    Forte, E.2    Mastronicola, D.3    Guffre, A.4    Arese, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.