Active sites of transition-metal enzymes with a focus on nickel

被引:110
作者
Ermler, U
Grabarse, W
Shima, S
Goubeaud, M
Thauer, RK
机构
[1] Max Planck Inst Biophys, D-60528 Frankfurt, Germany
[2] Univ Marburg, Max Planck Inst Terr Mikrobiol, D-35043 Marburg, Germany
[3] Univ Marburg, Mikrobiol Lab, D-35043 Marburg, Germany
关键词
D O I
10.1016/S0959-440X(98)80095-X
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
Since 1995, crystal structures have been determined for many transition-metal enzymes, in particular those containing the rarely used transition metals vanadium, molybdenum, tungsten, manganese, cobalt and nickel. Accordingly, our understanding of how an enzyme uses the unique properties of a specific transition metal has been substantially increased in the past few years. The different functions of nickel in catalysis are highlighted by describing the active sites of six nickel enzymes - methyl-coenyzme M reductase, urease, hydrogenase, superoxide dismutase, carbon monoxide dehydrogenase and acetyl-coenzyme A synthase.
引用
收藏
页码:749 / 758
页数:10
相关论文
共 99 条
  • [1] The "prismane" protein resolved:: X-ray structure at 1.7 Å and multiple spectroscopy of two novel 4Fe clusters
    Arendsen, AF
    Hadden, J
    Card, G
    McAlpine, AS
    Bailey, S
    Zaitsev, V
    Duke, EHM
    Lindley, PF
    Krockel, M
    Trautwein, AX
    Feiters, MC
    Charnock, JM
    Garner, CD
    Marritt, SJ
    Thomson, AJ
    Kooter, IM
    Johnson, MK
    van den Berg, WAM
    van Dongen, WMAM
    Hagen, WR
    [J]. JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 1998, 3 (01): : 81 - 95
  • [2] Methylation of carbon monoxide dehydrogenase from Clostridium thermoaceticum and mechanism of acetyl coenzyme A synthesis
    Barondeau, DP
    Lindahl, PA
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1997, 119 (17) : 3959 - 3970
  • [3] Activation of methyl-SCoM reductase to high specific activity after treatment of whole cells with sodium sulfide
    Becker, DF
    Ragsdale, SW
    [J]. BIOCHEMISTRY, 1998, 37 (08) : 2639 - 2647
  • [4] Crystal structure of formate dehydrogenase H: Catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster
    Boyington, JC
    Gladyshev, VN
    Khangulov, SV
    Stadtman, TC
    Sun, PD
    [J]. SCIENCE, 1997, 275 (5304) : 1305 - 1308
  • [5] CAMMACK R, 1998, BIOINORGANIC CATALYS, P231
  • [6] Crane BR, 1997, BIOCHEMISTRY-US, V36, P12120, DOI 10.1021/bi971066i
  • [7] Structure of nitric oxide synthase oxygenase dimer with pterin and substrate
    Crane, BR
    Arvai, AS
    Ghosh, DK
    Wu, CQ
    Getzoff, ED
    Stuehr, DJ
    Tainer, JA
    [J]. SCIENCE, 1998, 279 (5359) : 2121 - 2126
  • [8] Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 angstrom resolution
    Das, AK
    Helps, NR
    Cohen, PTW
    Barford, D
    [J]. EMBO JOURNAL, 1996, 15 (24) : 6798 - 6809
  • [9] Infrared spectroelectrochemical characterization of the [NiFe] hydrogenase of Desulfovibrio gigas
    deLacey, AL
    Hatchikian, EC
    Volbeda, A
    Frey, M
    FontecillaCamps, JC
    Fernandez, VM
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1997, 119 (31) : 7181 - 7189
  • [10] A multinuclear ENDOR study of the C-cluster in CO dehydrogenase from Clostridium thermoaceticum:: Evidence for HxO and histidine coordination to the [Fe4S4] center
    DeRose, VJ
    Telser, J
    Anderson, ME
    Lindahl, PA
    Hoffman, BM
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1998, 120 (34) : 8767 - 8776