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Volumn 119, Issue 43, 2015, Pages 13668-13674

FT-IR Characterization of the Light-Induced Ni-L2 and Ni-L3 States of [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYMES;

EID: 84946041646     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/acs.jpcb.5b03075     Document Type: Article
Times cited : (27)

References (50)
  • 1
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, Classification, and Biological Function of Hydrogenases: An Overview
    • Vignais, P. M.; Billoud, B. Occurrence, Classification, and Biological Function of Hydrogenases: An Overview Chem. Rev. 2007, 107, 4206-4272
    • (2007) Chem. Rev. , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 2
    • 35748956722 scopus 로고    scopus 로고
    • Activation and Inactivation of Hydrogenase Function and the Catalytic Cycle: Spectroelectrochemical Studies
    • De Lacey, A. L.; Fernández, V. M.; Rousset, M.; Cammack, R. Activation and Inactivation of Hydrogenase Function and the Catalytic Cycle: Spectroelectrochemical Studies Chem. Rev. 2007, 107, 4304-4330
    • (2007) Chem. Rev. , vol.107 , pp. 4304-4330
    • De Lacey, A.L.1    Fernández, V.M.2    Rousset, M.3    Cammack, R.4
  • 3
    • 35048826863 scopus 로고    scopus 로고
    • [NiFe] and [FeFe] Hydrogenases Studied by Advanced Magnetic Resonance Techniques
    • Lubitz, W.; Reijerse, E.; van Gastel, M. [NiFe] and [FeFe] Hydrogenases Studied by Advanced Magnetic Resonance Techniques Chem. Rev. 2007, 107, 4331-4365
    • (2007) Chem. Rev. , vol.107 , pp. 4331-4365
    • Lubitz, W.1    Reijerse, E.2    Van Gastel, M.3
  • 4
    • 70349289233 scopus 로고    scopus 로고
    • [NiFe] Hydrogenases: Structural and Spectroscopic Studies of the Reaction Mechanism
    • Ogata, H.; Lubitz, W.; Higuchi, Y. [NiFe] Hydrogenases: Structural and Spectroscopic Studies of the Reaction Mechanism Dalton Trans. 2009, 7577-7587
    • (2009) Dalton Trans. , pp. 7577-7587
    • Ogata, H.1    Lubitz, W.2    Higuchi, Y.3
  • 8
    • 0032483966 scopus 로고    scopus 로고
    • X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution
    • Peters, J. W.; Lanzilotta, W. N.; Lemon, B. J.; Seefeldt, L. C. X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution Science 1998, 282, 1853-1858
    • (1998) Science , vol.282 , pp. 1853-1858
    • Peters, J.W.1    Lanzilotta, W.N.2    Lemon, B.J.3    Seefeldt, L.C.4
  • 11
    • 0037009993 scopus 로고    scopus 로고
    • Structural Studies of the Carbon Monoxide Complex of [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F: Suggestion for the Initial Activation Site for Dihydrogen
    • Ogata, H.; Mizoguchi, Y.; Mizuno, N.; Miki, K.; Adachi, S.-i.; Yasuoka, N.; Yagi, T.; Yamauchi, O.; Hirota, S.; Higuchi, Y. Structural Studies of the Carbon Monoxide Complex of [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F: Suggestion for the Initial Activation Site for Dihydrogen J. Am. Chem. Soc. 2002, 124, 11628-11635
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11628-11635
    • Ogata, H.1    Mizoguchi, Y.2    Mizuno, N.3    Miki, K.4    Adachi, S.-I.5    Yasuoka, N.6    Yagi, T.7    Yamauchi, O.8    Hirota, S.9    Higuchi, Y.10
  • 13
    • 33747502852 scopus 로고    scopus 로고
    • Spectroelectrochemical Characterization of the [NiFe] Hydrogenase of Desulfovibrio vulgaris Miyazaki F
    • Fichtner, C.; Laurich, C.; Bothe, E.; Lubitz, W. Spectroelectrochemical Characterization of the [NiFe] Hydrogenase of Desulfovibrio vulgaris Miyazaki F Biochemistry 2006, 45, 9706-9716
    • (2006) Biochemistry , vol.45 , pp. 9706-9716
    • Fichtner, C.1    Laurich, C.2    Bothe, E.3    Lubitz, W.4
  • 14
    • 0017179533 scopus 로고
    • Properties of Purified Hydrogenase from the Particulate Fraction of Desulfovibrio vulgaris, Miyazaki
    • Yagi, T.; Kimura, K.; Daidoji, H.; Sakai, F.; Tamura, S. Properties of Purified Hydrogenase from the Particulate Fraction of Desulfovibrio vulgaris, Miyazaki J. Biochem. 1976, 79, 661-671
    • (1976) J. Biochem. , vol.79 , pp. 661-671
    • Yagi, T.1    Kimura, K.2    Daidoji, H.3    Sakai, F.4    Tamura, S.5
  • 16
    • 0034004792 scopus 로고    scopus 로고
    • Single Crystal EPR Studies of the Oxidized Active Site of [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F
    • Trofanchuk, O.; Stein, M.; Geßner, C.; Lendzian, F.; Higuchi, Y.; Lubitz, W. Single Crystal EPR Studies of the Oxidized Active Site of [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F J. Biol. Inorg. Chem. 2000, 5, 36-44
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 36-44
    • Trofanchuk, O.1    Stein, M.2    Geßner, C.3    Lendzian, F.4    Higuchi, Y.5    Lubitz, W.6
  • 17
    • 27644552110 scopus 로고    scopus 로고
    • Activation Process of [NiFe] Hydrogenase Elucidated by High-Resolution X-ray Analyses: Conversion of the Ready to the Unready State
    • Ogata, H.; Hirota, S.; Nakahara, A.; Komori, H.; Shibata, N.; Kato, T.; Kano, K.; Higuchi, Y. Activation Process of [NiFe] Hydrogenase Elucidated by High-Resolution X-ray Analyses: Conversion of the Ready to the Unready State Structure 2005, 13, 1635-1642
    • (2005) Structure , vol.13 , pp. 1635-1642
    • Ogata, H.1    Hirota, S.2    Nakahara, A.3    Komori, H.4    Shibata, N.5    Kato, T.6    Kano, K.7    Higuchi, Y.8
  • 19
    • 29544446001 scopus 로고    scopus 로고
    • A Single-Crystal ENDOR and Density Functional Theory Study of the Oxidized States of the [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F
    • van Gastel, M.; Stein, M.; Brecht, M.; Schröder, O.; Lendzian, F.; Bittl, R.; Ogata, H.; Higuchi, Y.; Lubitz, W. A Single-Crystal ENDOR and Density Functional Theory Study of the Oxidized States of the [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F J. Biol. Inorg. Chem. 2006, 11, 41-51
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 41-51
    • Van Gastel, M.1    Stein, M.2    Brecht, M.3    Schröder, O.4    Lendzian, F.5    Bittl, R.6    Ogata, H.7    Higuchi, Y.8    Lubitz, W.9
  • 21
    • 33645516017 scopus 로고    scopus 로고
    • Density Functional Study of the Catalytic Cycle of Nickel-Iron [NiFe] Hydrogenases and the Involvement of High-Spin Nickel(II)
    • Pardo, A.; De Lacey, A. L.; Fernández, V. M.; Fan, H.-J.; Fan, Y.; Hall, M. B. Density Functional Study of the Catalytic Cycle of Nickel-Iron [NiFe] Hydrogenases and the Involvement of High-Spin Nickel(II) J. Biol. Inorg. Chem. 2006, 11, 286-306
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 286-306
    • Pardo, A.1    De Lacey, A.L.2    Fernández, V.M.3    Fan, H.-J.4    Fan, Y.5    Hall, M.B.6
  • 23
    • 0037425515 scopus 로고    scopus 로고
    • Single Crystal EPR Studies of the Reduced Active Site of [NiFe] Hydrogenase from Desulfiovibrio vulgaris Miyazaki F
    • Foerster, S.; Stein, M.; Brecht, M.; Ogata, H.; Higuchi, Y.; Lubitz, W. Single Crystal EPR Studies of the Reduced Active Site of [NiFe] Hydrogenase from Desulfiovibrio vulgaris Miyazaki F J. Am. Chem. Soc. 2003, 125, 83-93
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 83-93
    • Foerster, S.1    Stein, M.2    Brecht, M.3    Ogata, H.4    Higuchi, Y.5    Lubitz, W.6
  • 24
    • 0034801480 scopus 로고    scopus 로고
    • Relativistic DFT Calculations of the Paramagnetic Intermediates of [NiFe] Hydrogenase. Implications for the Enzymatic Mechanism
    • Stein, M.; van Lenthe, E.; Baerends, E. J.; Lubitz, W. Relativistic DFT Calculations of the Paramagnetic Intermediates of [NiFe] Hydrogenase. Implications for the Enzymatic Mechanism J. Am. Chem. Soc. 2001, 123, 5839-5840
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5839-5840
    • Stein, M.1    Van Lenthe, E.2    Baerends, E.J.3    Lubitz, W.4
  • 25
    • 0033611949 scopus 로고    scopus 로고
    • Theoretical Characterization of the Reaction Intermediates in a Model of the Nickel-Iron Hydrogenase of Desulfovibrio gigas
    • Niu, S. Q.; Thomson, L. M.; Hall, M. B. Theoretical Characterization of the Reaction Intermediates in a Model of the Nickel-Iron Hydrogenase of Desulfovibrio gigas J. Am. Chem. Soc. 1999, 121, 4000-4007
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4000-4007
    • Niu, S.Q.1    Thomson, L.M.2    Hall, M.B.3
  • 26
    • 2542565159 scopus 로고    scopus 로고
    • Hydrogen-Induced Activation of the [NiFe]-Hydrogenase from Allochromatium vinosum as Studied by Stopped-Flow Infrared Spectroscopy
    • Kurkin, S.; George, S. J.; Thorneley, R. N. F.; Albracht, S. P. J. Hydrogen-Induced Activation of the [NiFe]-Hydrogenase from Allochromatium vinosum as Studied by Stopped-Flow Infrared Spectroscopy Biochemistry 2004, 43, 6820-6831
    • (2004) Biochemistry , vol.43 , pp. 6820-6831
    • Kurkin, S.1    George, S.J.2    Thorneley, R.N.F.3    Albracht, S.P.J.4
  • 28
    • 0029137283 scopus 로고
    • Stoichiometric Reductive Titrations of Desulfovibrio gigas Hydrogenase
    • Roberts, L. M.; Lindahl, P. A. Stoichiometric Reductive Titrations of Desulfovibrio gigas Hydrogenase J. Am. Chem. Soc. 1995, 117, 2565-2572
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2565-2572
    • Roberts, L.M.1    Lindahl, P.A.2
  • 29
    • 84928538572 scopus 로고    scopus 로고
    • Hydrogens Detected by Subatomic Resolution Protein Crystallography in a [NiFe] Hydrogenase
    • Ogata, H.; Nishikawa, K.; Lubitz, W. Hydrogens Detected by Subatomic Resolution Protein Crystallography in a [NiFe] Hydrogenase Nature 2015, 520, 517-574
    • (2015) Nature , vol.520 , pp. 517-574
    • Ogata, H.1    Nishikawa, K.2    Lubitz, W.3
  • 30
    • 0346308356 scopus 로고    scopus 로고
    • Wavelength Dependence of the Photo-Induced Conversion of the Ni-C to the Ni-L Redox State in the [NiFe] Hydrogenase of Desulfovibrio vulgaris Miyazaki F
    • Fichtner, C.; van Gastel, M.; Lubitz, W. Wavelength Dependence of the Photo-Induced Conversion of the Ni-C to the Ni-L Redox State in the [NiFe] Hydrogenase of Desulfovibrio vulgaris Miyazaki F Phys. Chem. Chem. Phys. 2003, 5, 5507-5513
    • (2003) Phys. Chem. Chem. Phys. , vol.5 , pp. 5507-5513
    • Fichtner, C.1    Van Gastel, M.2    Lubitz, W.3
  • 31
    • 0022420292 scopus 로고
    • Monovalent Nickel in Hydrogenase from Chromatium vinosum. Light Sensitivity and Evidence for Direct Interaction with Hydrogen
    • van der Zwaan, J. W.; Albracht, S. P. J.; Fontijn, R. D.; Slater, E. C. Monovalent Nickel in Hydrogenase from Chromatium vinosum. Light Sensitivity and Evidence for Direct Interaction with Hydrogen FEBS Lett. 1985, 179, 271-277
    • (1985) FEBS Lett. , vol.179 , pp. 271-277
    • Van Der Zwaan, J.W.1    Albracht, S.P.J.2    Fontijn, R.D.3    Slater, E.C.4
  • 32
  • 33
    • 0030608151 scopus 로고    scopus 로고
    • Studies of Light-Induced Nickel EPR Signals in Hydrogenase: Comparison of Enzymes with and without Selenium
    • Medina, M.; Hatchikian, E. C.; Cammack, R. Studies of Light-Induced Nickel EPR Signals in Hydrogenase: Comparison of Enzymes with and without Selenium Biochim. Biophys. Acta 1996, 1275, 227-236
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 227-236
    • Medina, M.1    Hatchikian, E.C.2    Cammack, R.3
  • 34
    • 70349881886 scopus 로고    scopus 로고
    • FTIR Study on the Light Sensitivity of the [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F: Ni-C to Ni-L Photoconversion, Kinetics of Proton Rebinding and H/D Isotope Effect
    • Kellers, P.; Pandelia, M.-E.; Currell, L. J.; Gorner, H.; Lubitz, W. FTIR Study on the Light Sensitivity of the [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F: Ni-C to Ni-L Photoconversion, Kinetics of Proton Rebinding and H/D Isotope Effect Phys. Chem. Chem. Phys. 2009, 11, 8680-8683
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 8680-8683
    • Kellers, P.1    Pandelia, M.-E.2    Currell, L.J.3    Gorner, H.4    Lubitz, W.5
  • 35
    • 0029066353 scopus 로고
    • Infrared-Detectable Groups Sense Changes in Charge Density on the Nickel Center in Hydrogenase from Chromatium vinosum
    • Bagley, K. A.; Duin, E. C.; Roseboom, W.; Albracht, S. P. J.; Woodruff, W. H. Infrared-Detectable Groups Sense Changes in Charge Density on the Nickel Center in Hydrogenase from Chromatium vinosum Biochemistry 1995, 34, 5527-5535
    • (1995) Biochemistry , vol.34 , pp. 5527-5535
    • Bagley, K.A.1    Duin, E.C.2    Roseboom, W.3    Albracht, S.P.J.4    Woodruff, W.H.5
  • 37
    • 84874979548 scopus 로고    scopus 로고
    • A Metal-Metal Bond in the Light-Induced State of [NiFe] Hydrogenases with Relevance to Hydrogen Evolution
    • Kampa, M.; Pandelia, M. E.; Lubitz, W.; van Gastel, M.; Neese, F. A Metal-Metal Bond in the Light-Induced State of [NiFe] Hydrogenases with Relevance to Hydrogen Evolution J. Am. Chem. Soc. 2013, 135, 3915-3925
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 3915-3925
    • Kampa, M.1    Pandelia, M.E.2    Lubitz, W.3    Van Gastel, M.4    Neese, F.5
  • 38
    • 0030498648 scopus 로고    scopus 로고
    • Spin-Spin Interactions between the Ni Site and the [4Fe-4S] Centers as a Probe of Light-Induced Structural Changes in Active Desulfovibrio gigas Hydrogenase
    • Dole, F.; Medina, M.; More, C.; Cammack, R.; Bertrand, P.; Guigliarelli, B. Spin-Spin Interactions between the Ni Site and the [4Fe-4S] Centers as a Probe of Light-Induced Structural Changes in Active Desulfovibrio gigas Hydrogenase Biochemistry 1996, 35, 16399-16406
    • (1996) Biochemistry , vol.35 , pp. 16399-16406
    • Dole, F.1    Medina, M.2    More, C.3    Cammack, R.4    Bertrand, P.5    Guigliarelli, B.6
  • 39
    • 84918828153 scopus 로고    scopus 로고
    • a States by the Redox State of the Proximal Fe-S Cluster in the Catalytic Cycle of [NiFe] Hydrogenase
    • a States by the Redox State of the Proximal Fe-S Cluster in the Catalytic Cycle of [NiFe] Hydrogenase Angew. Chem., Int. Ed. 2014, 53, 13817-13820
    • (2014) Angew. Chem., Int. Ed. , vol.53 , pp. 13817-13820
    • Tai, H.1    Nishikawa, K.2    Suzuki, M.3    Higuchi, Y.4    Hirota, S.5
  • 41
    • 0033807920 scopus 로고    scopus 로고
    • The Bio-Organometallic Chemistry of Active Site Iron in Hydrogenases
    • Darensbourg, M. Y.; Lyon, E. J.; Smee, J. J. The Bio-Organometallic Chemistry of Active Site Iron in Hydrogenases Coord. Chem. Rev. 2000, 206, 533-561
    • (2000) Coord. Chem. Rev. , vol.206 , pp. 533-561
    • Darensbourg, M.Y.1    Lyon, E.J.2    Smee, J.J.3
  • 42
    • 84904428766 scopus 로고    scopus 로고
    • Resonance Raman Spectroscopy on [NiFe] Hydrogenase Provides Structural Insights into Catalytic Intermediates and Reactions
    • Horch, M.; Schoknecht, J.; Mroginski, M. A.; Lenz, O.; Hildebrandt, P.; Zebger, I. Resonance Raman Spectroscopy on [NiFe] Hydrogenase Provides Structural Insights into Catalytic Intermediates and Reactions J. Am. Chem. Soc. 2014, 136, 9870-9873
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 9870-9873
    • Horch, M.1    Schoknecht, J.2    Mroginski, M.A.3    Lenz, O.4    Hildebrandt, P.5    Zebger, I.6
  • 43
    • 38549139111 scopus 로고    scopus 로고
    • Proton Pathways in a [NiFe]-Hydrogenase: A Theoretical Study
    • Teixeira, V. H.; Soares, C. M.; Baptista, A. M. Proton Pathways in a [NiFe]-Hydrogenase: A Theoretical Study Proteins 2008, 70, 1010-1022
    • (2008) Proteins , vol.70 , pp. 1010-1022
    • Teixeira, V.H.1    Soares, C.M.2    Baptista, A.M.3
  • 44
    • 50849141732 scopus 로고    scopus 로고
    • A QM/MM Study of Proton Transport Pathways in a [NiFe] Hydrogenase
    • Galván, I. F.; Volbeda, A.; Fontecilla-Camps, J. C.; Field, M. J. A QM/MM Study of Proton Transport Pathways in a [NiFe] Hydrogenase Proteins 2008, 73, 195-203
    • (2008) Proteins , vol.73 , pp. 195-203
    • Galván, I.F.1    Volbeda, A.2    Fontecilla-Camps, J.C.3    Field, M.J.4
  • 47
    • 84872381995 scopus 로고    scopus 로고
    • Photosensitivity of the Ni-A State of [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F with Visible Light
    • Osuka, H.; Shomura, Y.; Komori, H.; Shibata, N.; Nagao, S.; Higuchi, Y.; Hirota, S. Photosensitivity of the Ni-A State of [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F with Visible Light Biochem. Biophys. Res. Commun. 2013, 430, 284-288
    • (2013) Biochem. Biophys. Res. Commun. , vol.430 , pp. 284-288
    • Osuka, H.1    Shomura, Y.2    Komori, H.3    Shibata, N.4    Nagao, S.5    Higuchi, Y.6    Hirota, S.7
  • 48
    • 84871552098 scopus 로고    scopus 로고
    • A Functional [NiFe]-Hydrogenase Model Compound That Undergoes Biologically Relevant Reversible Thiolate Protonation
    • Weber, K.; Krämer, T.; Shafaat, H. S.; Weyhermüller, T.; Bill, E.; van Gastel, M.; Neese, F.; Lubitz, W. A Functional [NiFe]-Hydrogenase Model Compound That Undergoes Biologically Relevant Reversible Thiolate Protonation J. Am. Chem. Soc. 2012, 134, 20745-20755
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 20745-20755
    • Weber, K.1    Krämer, T.2    Shafaat, H.S.3    Weyhermüller, T.4    Bill, E.5    Van Gastel, M.6    Neese, F.7    Lubitz, W.8
  • 50
    • 37049132354 scopus 로고
    • Thermodynamic Considerations in Coordination. Part XI. Enthalpies and Entropies of Protonating Asparaginyl, Aspartyl, Cysteinyl, and Phemylalanyl Anions
    • Graham, R. D.; William, D. R.; Yeo, P. A. Thermodynamic Considerations in Coordination. Part XI. Enthalpies and Entropies of Protonating Asparaginyl, Aspartyl, Cysteinyl, and Phemylalanyl Anions J. Chem. Soc., Perkin Trans. 2 1972, 1876-1877
    • (1972) J. Chem. Soc., Perkin Trans. 2 , pp. 1876-1877
    • Graham, R.D.1    William, D.R.2    Yeo, P.A.3


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