Structural highlights
FunctionPublication Abstract from PubMedHydrogenases display a wide range of catalytic rates and biases in reversible hydrogen gas oxidation catalysis. The interac-tions of the iron-sulfur containing catalytic site with the local protein environment are thought to contribute to differences in catalytic reactivity, but this has not been demonstrated. The microbe Clostridium pasteurianum produces three [FeFe]-hydrogenases that differ in "catalytic bias" by exerting a disproportionate rate acceleration in one direction or the other that spans a remarkable six orders of magnitude. The combination of high-resolution structural work, biochemical analyses, and computational modeling indicate that protein secondary interactions directly influence the relative stabiliza-tion/destabilization of different oxidation states of the active site metal cluster. This selective stabilization or destabilization of oxidation states can preferentially promote hydrogen oxidation or proton reduction and represents a simple yet elegant model by which a protein catalytic site can confer catalytic bias. Tuning catalytic bias of hydrogen gas producing hydrogenases.,Artz JH, Zadvornyy OA, Mulder DW, Keable SM, Cohen AE, Ratzloff MW, Williams SG, Ginovska B, Kumar N, Song J, McPhillips SE, Davidson C, Lyubimov AY, Pence N, Schut GJ, Jones AK, Soltis SM, Adams M, Raugei S, King PW, Peters JW J Am Chem Soc. 2019 Dec 9. doi: 10.1021/jacs.9b08756. PMID:31816235[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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