[NiFe] hydrogenases from the hyperthermophilic bacterium Aquifex aeolicus: properties, function, and phylogenetics

Brugna-Guiral, Marianne and Tron, Pascale and Nitschke, Wolfgang and Stetter, Karl Otto and Burlat, Benedicte and Guigliarelli, Bruno and Bruschi, Mireille and Giudici-Orticoni, Marie Thérèse (2003) [NiFe] hydrogenases from the hyperthermophilic bacterium Aquifex aeolicus: properties, function, and phylogenetics. EXTREMOPHILES, 7 (2). pp. 145-157. ISSN 1431-0651, 1433-4909

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Abstract

Genes potentially coding for three distinct [NiFe] hydrogenases are present in the genome of Aquifex aeolicus. We have demonstrated that all three hydrogenases are expressed under standard growth conditions of the organism. Two hydrogenases were further purified to homogeneity. A periplasmically oriented hydrogenase was obtained in two forms, i.e., as a soluble enzyme containing only the two essential subunits and as a detergent-solubilized complex additionally containing a membrane-integral h-type cytochrome. The second hydrogenase purified was identified as a soluble cytoplasmic enzyme. The isolated enzymes were characterized with respect to biochemical/biophysical parameters, activity, thermostability, and substrate specificity. The phylogenetic positioning of all three hydrogenases was analyzed. A model for the metabolic roles of the three enzymes is proposed on the basis of the obtained results.

Item Type: Article
Uncontrolled Keywords: NADH-UBIQUINONE OXIDOREDUCTASE; ARCHAEON PYROCOCCUS-FURIOSUS; MEMBRANE-BOUND HYDROGENASE; COMPLEX-I; FERREDOXIN OXIDOREDUCTASE; THIOCAPSA-ROSEOPERSICINA; WOLINELLA-SUCCINOGENES; DESULFOVIBRIO-GIGAS; PURIFICATION; ARCHAEBACTERIUM; Aquifex aeolicus; hydrogenase; phylogeny; hydrogen metabolism
Subjects: 500 Science > 570 Life sciences
Divisions: Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum)
Depositing User: Dr. Gernot Deinzer
Date Deposited: 17 Aug 2021 12:15
Last Modified: 17 Aug 2021 12:15
URI: https://pred.uni-regensburg.de/id/eprint/39147

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