Activation and deactivation of the membrane-bound hydrogenase from Desulfovibrio desulfuricans, Norway strain |
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| Authors: | V M Fernandez K K Rao M A Fernandez R Cammack |
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| Affiliation: | 1. Department of Surgery, University of Kansas Medical Center, Kansas City, Kansas, USA;2. Department of Surgery, Creighton University Medical Center, Omaha, Nebraska, USA;3. CHS International, Cape Canaveral, Florida, USA;1. Polytechnic University of Timisoara, Victoriei Square, nr. 2, 300006 Timisoara, Romania;2. Hungarian Academy of Sciences, Biological Research Centre Szeged, Temesvari krt. 62, 6726 Szeged, Hungary;3. Seqomics Biotechnology Ltd., Vállalkozók útja 7, 6782 Mórahalom, Hungary;4. Szent István University, Faculty of Economics, Agricultural and Health Studies, Szarvas, Hungary;1. Department of Botany, Centre of Advanced Study in Botany, Institute of Science, Banaras Hindu University, Varanasi 221005, India;2. Molecular Biology Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400085, India;3. Division of Glycoscience, Department of Chemistry, School of Engineering Sciences in Chemistry, Biotechnology and Health, Royal Institute of Technology (KTH), AlbaNova University Centre, Stockholm 10691, Sweden;4. Homi Bhabha National Institute, Anushakti Nagar, Mumbai 400094, India |
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| Abstract: | The hydrogenase from D. desulfuricans, when isolated in air, had a low activity in the hydrogen-methyl viologen reductase assay, and no activity in the hydrogen-methylene blue reductase assay. The activity increased markedly during incubation under hydrogen. This process is interpreted in terms of conversion of the enzyme from a relatively inactive Unready state to the Active state. Oxidation by dichloro-indophenol caused conversion to a state in which the hydrogen-uptake activity to methyl viologen was preserved, but hydrogen-methylene blue activity was not. This form is termed the Ready state. This behaviour resembles that of the hydrogenase of Desulfovibrio gigas and thus may be a widespread property of this class of hydrogenases. The electron-spin-resonance spectra of the D. desulfuricans enzyme showed the presence of [3Fe-xS] and [4Fe-4S] clusters. Spectra were also observed in the various states of activation of the enzyme. In these respects, the hydrogenase of D. desulfuricans resembles that from D. gigas, although the latter may have an additional iron-sulphur cluster. |
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