Reactions of H2, CO, and O2 with active [NiFe]-Hydrogenase from Allochromatium vinosum.: A stopped-flow infrared study

被引:89
作者
George, SJ
Kurkin, S
Thorneley, RNF
Albracht, SPJ
机构
[1] John Innes Ctr, Dept Biol Chem, Norwich NR4 7UH, Norfolk, England
[2] Univ Amsterdam, Swammerdam Inst Life Sci, NL-1018 TV Amsterdam, Netherlands
关键词
D O I
10.1021/bi049853k
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Ni-Fe site in the active membrane-bound [NiFe]-hydrogenase from Allochromatium vinosum can exist in three different redox states. In the most oxidized state (Ni-a-S) the nickel is divalent. The most reduced state (Ni-a-SR) likewise has Ni2+, while the intermediate state (Ni-a-C*) has Ni3+. The transitions between these states have been studied by stopped-flow Fourier transform infrared spectroscopy. It is inferred from the data that the Ni-a-S --> Ni-a-C* and Ni-a-C* --> Ni-a-SR transitions induced by dihydrogen require one of the [4Fe-4S] clusters to be oxidized. Enzyme in the Ni-a-S state with all of the iron-sulfur clusters reduced reacts with dihydrogen to form the Ni-a-SR state in milliseconds. By contrast, when one of the cubane clusters is oxidized, the Ni-a-S state reacts with dihydrogen to form the Ni-a-C* state with all of the iron-sulfur clusters reduced. The competition between dihydrogen and carbon monoxide for binding to the active site was dependent on the redox state of the nickel ion. Formation of the Ni-a-S.CO state (Ni2+) by reacting CO with enzyme in the Ni-a-SR and Ni-a-S states (Ni2+) is considerably faster than its formation from enzyme in the Ni-a-C* (Ni3+) state. Excess oxygen converted hydrogen-reduced enzyme to the inactive Ni-r* state within 158 ms, suggesting a direct reaction at the Ni-Fe site. With lower O-2 concentrations the formation of intermediate states was observed. The results are discussed in the light of the present knowledge of the structure and mechanism of action of the A. vinosum enzyme.
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页码:6808 / 6819
页数:12
相关论文
共 34 条
  • [21] Hydrogen-induced activation of the [NiFe]-hydrogenase from Allochromatium vinosum as studied by stopped-flow infrared spectroscopy
    Kurkin, S
    George, SJ
    Thorneley, RNF
    Albracht, SPJ
    [J]. BIOCHEMISTRY, 2004, 43 (21) : 6820 - 6831
  • [22] Stopped-flow Fourier transform infrared spectroscopy of nitromethane oxidation by the diiron(IV) intermediate of methane monooxygenase
    Muthusamy, M
    Ambundo, EA
    George, SJ
    Lippard, SJ
    Thorneley, RNF
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2003, 125 (37) : 11150 - 11151
  • [23] 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
    Yasuoka, N
    Yagi, T
    Yamauchi, O
    Hirota, S
    Higuchi, Y
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (39) : 11628 - 11635
  • [24] Catalytic electron transport in Chromatium vinosum [NiFe]-hydrogenase:: Application of voltammetry in detecting redox-active centers and establishing that hydrogen oxidation is very fast even at potentials close to the reversible H+/H2 value
    Pershad, HR
    Duff, JLC
    Heering, HA
    Duin, EC
    Albracht, SPJ
    Armstrong, FA
    [J]. BIOCHEMISTRY, 1999, 38 (28) : 8992 - 8999
  • [25] Characterization of the active site of a hydrogen sensor from Alcaligenes eutrophus
    Pierik, AJ
    Schmelz, M
    Lenz, O
    Friedrich, B
    Albracht, SPJ
    [J]. FEBS LETTERS, 1998, 438 (03) : 231 - 235
  • [26] Interactions of Se-77 and (CO)-C-13 with nickel in the active site of active F-420-nonreducing hydrogenase from Methanococcus voltae
    Sorgenfrei, O
    Duin, EC
    Klein, A
    Albracht, SPJ
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (39) : 23799 - 23806
  • [27] FURTHER CHARACTERIZATION OF THE SPIN COUPLING OBSERVED IN OXIDIZED HYDROGENASE FROM CHROMATIUM-VINOSUM - A MOSSBAUER AND MULTIFREQUENCY EPR STUDY
    SURERUS, KK
    CHEN, M
    VANDERZWAAN, JW
    RUSNAK, FM
    KOLK, M
    DUIN, EC
    ALBRACHT, SPJ
    MUNCK, E
    [J]. BIOCHEMISTRY, 1994, 33 (16) : 4980 - 4993
  • [28] Thorneley RNF, 2000, PROKARYOTIC NITROGEN FIXATION, P81
  • [29] MONO-VALENT NICKEL IN HYDROGENASE FROM CHROMATIUM-VINOSUM - LIGHT SENSITIVITY AND EVIDENCE FOR DIRECT INTERACTION WITH HYDROGEN
    VANDERZWAAN, JW
    ALBRACHT, SPJ
    FONTIJN, RD
    SLATER, EC
    [J]. FEBS LETTERS, 1985, 179 (02): : 271 - 277
  • [30] EFFECT OF O-17(2) AND (CO)-C-13 ON EPR-SPECTRA OF NICKEL IN HYDROGENASE FROM CHROMATIUM-VINOSUM
    VANDERZWAAN, JW
    COREMANS, JMCC
    BOUWENS, ECM
    ALBRACHT, SPJ
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1990, 1041 (02) : 101 - 110