Hydrogenases from the hyperthermophilic bacterium Aquifex aeolicus:: Electrocatalysis of the hydrogen production/consumption reactions at carbon electrodes

被引:16
作者
Lojou, É [1 ]
Giudici-Orticoni, MT [1 ]
Bianco, P [1 ]
机构
[1] CNRS, Inst Biol Struct & Microbiol, Unite Bioenerget & Ingn Prot, F-13402 Marseille, France
关键词
Aquifex aeolicus; hyperthermophiles; voltammetry; hydrogenase;
D O I
10.1016/j.jelechem.2004.11.016
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
Two [NiFe] hydrogenases extracted from the hyperthermophilic bacterium Aquifex aeolicus (Aa) are studied at a pyrolytic graphite electrode using cyclic voltammetry. The two hydrogenases have been shown to exhibit very similar behavior. They are able to catalyze under a nitrogen or a hydrogen atmosphere, the direct hydrogen production from protons and the reverse reaction of hydrogen oxidation directly in the absence of any promoter. The effect of experimental parameters (enzyme concentration, pH, ionic strength) are investigated. The electrocatalytic activity has been shown to increase when the temperature is increased within the range 22-65 degrees C in agreement with the evolution of the enzymatic activity. Using electrochemical techniques concomitantly with quartz crystal microgravimetry, it is demonstrated that the electrocatalysis is largely governed by the strong adsorption of hydrogenases on the electrode surface. The similarity between the two Aa hydrogenases and the hydrogenase from another hyperthermophilic bacterium, Pyrococcus furiosus, is discussed. (c) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码:79 / 86
页数:8
相关论文
共 40 条
[1]   Finding and using hyperthermophilic enzymes [J].
Adams, MWW ;
Kelly, RM .
TRENDS IN BIOTECHNOLOGY, 1998, 16 (08) :329-332
[2]  
ADAMS MWW, 1994, FEMS MICROBIOL REV, V15, P261, DOI 10.1111/j.1574-6976.1994.tb00139.x
[3]   THE STRUCTURE AND MECHANISM OF IRON-HYDROGENASES [J].
ADAMS, MWW .
BIOCHIMICA ET BIOPHYSICA ACTA, 1990, 1020 (02) :115-145
[4]  
[Anonymous], BIOCHIM BIOPHYS ACTA
[5]   Cytochromes c555 from the hyperthermophilic bacterium Aquifex aeolicus.: 2.: Heterologous production of soluble cytochrome c555s and investigation of the role of methionine residues [J].
Aubert, C ;
Guerlesquin, F ;
Bianco, P ;
Leroy, G ;
Tron, P ;
Stetter, KO ;
Bruschi, M .
BIOCHEMISTRY, 2001, 40 (45) :13690-13698
[6]   Cytochromes c555 from the hyperthermophilic bacterium Aquifex aeolicus (VF5).: 1.: Characterization of two highly homologous, soluble and membranous, cytochromes c555 [J].
Baymann, F ;
Tron, P ;
Schoepp-Cothenet, B ;
Aubert, C ;
Bianco, P ;
Stetter, KO ;
Nitschke, W ;
Schütz, M .
BIOCHEMISTRY, 2001, 40 (45) :13681-13689
[7]   REACTIVITY OF [FE] AND [NI-FE-SE] HYDROGENASES WITH THEIR OXIDOREDUCTION PARTNER - THE TETRAHEME CYTOCHROME-C3 [J].
BIANCO, P ;
HALADJIAN, J ;
BRUSCHI, M ;
GUERLESQUIN, F .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1992, 189 (02) :633-639
[8]   ELECTROCATALYSIS AT HYDROGENASE OR CYTOCHROME C-3-MODIFIED GLASSY-CARBON ELECTRODES [J].
BIANCO, P ;
HALADJIAN, J .
ELECTROANALYSIS, 1991, 3 (09) :973-977
[9]   ELECTROCATALYTIC HYDROGEN-EVOLUTION AT THE PYROLYTIC-GRAPHITE ELECTRODE IN THE PRESENCE OF HYDROGENASE [J].
BIANCO, P ;
HALADJIAN, J .
JOURNAL OF THE ELECTROCHEMICAL SOCIETY, 1992, 139 (09) :2428-2432
[10]   [NiFe] hydrogenases from the hyperthermophilic bacterium Aquifex aeolicus:: properties, function, and phylogenetics [J].
Brugna-Guiral, M ;
Tron, P ;
Nitschke, W ;
Stetter, KO ;
Burlat, B ;
Guigliarelli, B ;
Bruschi, M ;
Giudici-Orticoni, MT .
EXTREMOPHILES, 2003, 7 (02) :145-157