Hyperthermostable and oxygen resistant hydrogenases from a hyperthermophilic bacterium Aquifex aeolicus:: Physicochemical properties

被引：34
作者：
Guiral, Marianne [1 ]
Tron, Pascale [1 ]
Belle, Valrie [1 ]
Aubert, Corinne [1 ]
Léger, Christophe [1 ]
Guigliarelli, Bruno [1 ]
Giudici-Orticoni, Marie-Therese [1 ]
机构：
[1] CNRS, IBSM, BIP, Lab Bioenerget & Ingn Prot, F-13402 Marseille 20, France
来源：
INTERNATIONAL JOURNAL OF HYDROGEN ENERGY | 2006年 / 31卷 / 11期
关键词：
Aquifex aeolicus; hydrogenase; thermal stability; oxygen resistant;
D O I：
10.1016/j.ijhydene.2006.06.007
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
The discovery of hydrogenases in hyperthermophiles has important ramifications not only in microbial physiology and evolution but also in biotechnologies. These organisms are the source of extremely stable enzymes (regarding temperature, pressure, and 02). Aquifex aeolicus is a microaerophilic, hyperthermophilic bacterium containing three [NiFe] hydrogenases. It is the most hyperthermophilic bacterium known to date and grows at 85 degrees C under a H-2/CO2/O-2 atmosphere. The Aquificales represent the earliest branching order of the bacterial domain indicating that they are the most ancient bacteria. Two Aquifex hydrogenases (one membrane-bound and one soluble) have been purified and characterized. In contrast to the majority of the [NiFe] hydrogenases, the hydrogenases from A. aeolicus are rather tolerant to oxygen. The molecular basis of the oxygen resistance of Aquifex hydrogenases has been investigated. The great stability of Aquifex hydrogenases with respect to oxygen and high temperatures make these enzymes good candidates for biotechnological uses. (c) 2006 International Association for Hydrogen Energy. Published by Elsevier Ltd. All rights reserved.
引用
收藏
页码：1424 / 1431
页数：8
相关论文
共 23 条
  • [1] ADAMS MWW, 1994, FEMS MICROBIOL REV, V15, P261, DOI 10.1111/j.1574-6976.1994.tb00139.x
  • [2] The H2 sensor of Ralstonia eutropha -: Biochemical characteristics, spectroscopic properties, and its interaction with a histidine protein kinase
    Bernhard, M
    Buhrke, T
    Bleijlevens, B
    De Lacey, AL
    Fernandez, VM
    Albracht, SPJ
    Friedrich, B
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (19) : 15592 - 15597
  • [3] SEQUENCES AND CHARACTERIZATION OF HUPU AND HUPV GENES OF BRADYRHIZOBIUM-JAPONICUM ENCODING A POSSIBLE NICKEL-SENSING COMPLEX INVOLVED IN HYDROGENASE EXPRESSION
    BLACK, LK
    FU, CL
    MAIER, RJ
    [J]. JOURNAL OF BACTERIOLOGY, 1994, 176 (22) : 7102 - 7106
  • [4] The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of Ralstonia eutropha H16 by way of a cyanide ligand to nickel
    Bleijlevens, B
    Buhrke, T
    van der Linden, E
    Friedrich, B
    Albracht, SPJ
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (45) : 46686 - 46691
  • [5] [NiFe] hydrogenases from the hyperthermophilic bacterium Aquifex aeolicus:: properties, function, and phylogenetics
    Brugna-Guiral, M
    Tron, P
    Nitschke, W
    Stetter, KO
    Burlat, B
    Guigliarelli, B
    Bruschi, M
    Giudici-Orticoni, MT
    [J]. EXTREMOPHILES, 2003, 7 (02) : 145 - 157
  • [6] Oxygen tolerance of the H2-sensing [NiFe] hydrogenase from Ralstonia eutropha H16 is based on limited access of oxygen to the active site
    Buhrke, T
    Lenz, O
    Krauss, N
    Friedrich, B
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (25) : 23791 - 23796
  • [7] Reduction of unusual iron-sulfur clusters in the H2-sensing regulatory Ni-Fe hydrogenase from Ralstonia eutropha H16
    Buhrke, T
    Löscher, S
    Lenz, O
    Schlodder, E
    Zebger, I
    Andersen, LK
    Hildebrandt, P
    Meyer-Klaucke, W
    Dau, H
    Friedrich, B
    Haumann, M
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (20) : 19488 - 19495
  • [8] The complete genome of the hyperthermophilic bacterium Aquifex aeolicus
    Deckert, G
    Warren, PV
    Gaasterland, T
    Young, WG
    Lenox, AL
    Graham, DE
    Overbeek, R
    Snead, MA
    Keller, M
    Aujay, M
    Huber, R
    Feldman, RA
    Short, JM
    Olsen, GJ
    Swanson, RV
    [J]. NATURE, 1998, 392 (6674) : 353 - 358
  • [9] Enlarging the gas access channel to the active site renders the regulatory hydrogenase HupUV of Rhodobacter capsulatus O2 sensitive without affecting its transductory activity
    Duché, O
    Elsen, S
    Cournac, L
    Colbeau, A
    [J]. FEBS JOURNAL, 2005, 272 (15) : 3899 - 3908
  • [10] Hydrogen metabolism in the hyperthermophilic bacterium Aquifex aeolicus
    Guiral, M
    Aubert, T
    Giudici-Orticoni, MT
    [J]. BIOCHEMICAL SOCIETY TRANSACTIONS, 2005, 33 : 22 - 24
123