On the prosthetic groups of the NiFe sulfhydrogenase from Pyrococcus furiosus: topology, structure, and temperature-dependent redox chemistry |
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Authors: | Pedro J Silva Baltazar de Castro W R Hagen |
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Institution: | (1) Wageningen University, Laboratory of Biochemistry Bioinorganic Chemistry Group, Dreijenlaan 3, NL-6703 HA Wageningen, The Netherlands e-mail: fred.hagen@epr.bc.wau.nl Fax: +31-317-484801, NL;(2) CEQUP, Departamento de Química, Faculdade de Ciências Rua do Campo Alegre 687, P-4150 Porto, Portugal, PT |
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Abstract: | The sulfhydrogenase complex of Pyrococcus furiosus is an αβγδ heterotetramer with both hydrogenase activity (borne by the αδ subunits) and sulfur reductase activity (carried
by the βγ subunits). The β-subunit contains at least two 4Fe-4S] cubanes and the γ-subunit contains one 2Fe-2S] cluster
and one FAD molecule. The δ-subunit contains three 4Fe-4S] cubanes and the α-subunit carries the NiFe dinuclear center. Only
three Fe/S signals are observed in EPR-monitored reduction by dithionite, NADPH, or internal substrate upon heating. All other
clusters presumably have reduction potentials well below that of the H+/H2 couple. Heat-induced reduction by internal substrate allows, for the first time, EPR monitoring of the NiFe center in a hyperthermophilic
hydrogenase, which passes through a number of states, some of which are similar to states previously defined for mesophilic
hydrogenases. The complexity of the observed transitions reflects a combination of temperature-dependent activation and temperature-dependent
reduction potentials.
Received: 10 December 1998 / Accepted: 16 February 1999 |
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Keywords: | Hydrogenase Nickel Iron-sulfur Hyperthermophilic organisms Electron paramagnetic resonance |
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