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- W2030903556 abstract "Hydrogenases have been purified from different biological sources. They are highly diversified enzymes in terms of active centers constitution, although they catalyze the simplest oxidation-reduction process: H2 ⇌ 2H+ + 2e. Hydrogenases have been recognized so far to be ironsulfur proteins. Generally they contain from four to twelve atoms of non-haem iron arranged in FeS clusters representative of the known basic structures, e.g., [2Fe-2S], 3Fe-xS], and [4Fe-4S] [1–7]. Recently, nickel joined the group of transition metals relevant in biological oxidation-reduction processes. It was shown to be a structural component of the hydrogenases isolated from Desulfovibriogigas [1, 2], Desulfovibrio desulfuricans (ATTC 27774) [3], Desulfovibrio desulfuricans (Norway strain) [4], Methanosarcina barkeri [5], Methanobacteriumthermoautotrophicum [6] and Chromatium vinosum [8]. With the exception of the last one, they were demonstrated to contain EPR nickel redox dependent signals. As an example, D. gigas hydrogenase exhibits rhombic EPR signals, with g-values 2.31, 2.23 and 2.02 (see Fig. 1). Using isotopic reconstitution by 61Ni (nuclear magnetic moment I = 32), the EPR signal was proven arise from a nickel species [9]. The same types of experiments were reported for M. thermoautotrophicum [6] and D. desulfuricans (ATCC 27774) hydrogenases [3]. A detailed EPR study on the oxidation-reduction transition of the EPR detectable species in the presence of reductant (dithionite and hydrogen) indicates [1, 2]: The reduction of the Ni EPR active species is an one-electron process (possibly associated with the redox couple Ni(III)Ni(II)). No evidence was found so far for exchangeable protons in the vicinity of the nickel center in the oxidized (native) state. However, hydrogen reduced samples originate a different EPR rhombic Ni signal, which may represent an active transient species occurring during the activation of hydrogen molecules [9]. Thus, it is attractive to propose the presence of a hydride intermediate in analogy with nickel catalysts involved in hydrogenation processes [10]. Although the determined mid-point redox potential (−220 mV) is more negative than that expected for nickel compounds [11] it is still more positive than that of the substrate couple H2/H+. The value determined was shown to be pH dependent [2]." @default.
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- W2030903556 date "1983-01-01" @default.
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- W2030903556 title "Nickel containing hydrogenases" @default.
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- W2030903556 doi "https://doi.org/10.1016/s0020-1693(00)95032-1" @default.
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