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Tuning Catalytic Bias of Hydrogen Gas Producing Hydrogenases.

Identifieur interne : 000007 ( Main/Exploration ); précédent : 000006; suivant : 000008

Tuning Catalytic Bias of Hydrogen Gas Producing Hydrogenases.

Auteurs : Jacob H. Artz [États-Unis] ; Oleg A. Zadvornyy [États-Unis] ; David W. Mulder [États-Unis] ; Stephen M. Keable [États-Unis] ; Aina E. Cohen [États-Unis] ; Michael W. Ratzloff [États-Unis] ; S Garrett Williams [États-Unis] ; Bojana Ginovska [États-Unis] ; Neeraj Kumar [États-Unis] ; Jinhu Song [États-Unis] ; Scott E. Mcphillips [États-Unis] ; Catherine M. Davidson [États-Unis] ; Artem Y. Lyubimov [États-Unis] ; Natasha Pence [États-Unis] ; Gerrit J. Schut [États-Unis] ; Anne K. Jones [États-Unis] ; S Michael Soltis [États-Unis] ; Michael W W. Adams [États-Unis] ; Simone Raugei [États-Unis] ; Paul W. King [États-Unis] ; John W. Peters [États-Unis]

Source :

RBID : pubmed:31816235

Abstract

Hydrogenases display a wide range of catalytic rates and biases in reversible hydrogen gas oxidation catalysis. The interactions 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 6 orders of magnitude. The combination of high-resolution structural work, biochemical analyses, and computational modeling indicates that protein secondary interactions directly influence the relative stabilization/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.

DOI: 10.1021/jacs.9b08756
PubMed: 31816235


Affiliations:


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Le document en format XML

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<div type="abstract" xml:lang="en">Hydrogenases display a wide range of catalytic rates and biases in reversible hydrogen gas oxidation catalysis. The interactions 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
<i>Clostridium pasteurianum</i>
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 6 orders of magnitude. The combination of high-resolution structural work, biochemical analyses, and computational modeling indicates that protein secondary interactions directly influence the relative stabilization/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.</div>
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<AbstractText>Hydrogenases display a wide range of catalytic rates and biases in reversible hydrogen gas oxidation catalysis. The interactions 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
<i>Clostridium pasteurianum</i>
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 6 orders of magnitude. The combination of high-resolution structural work, biochemical analyses, and computational modeling indicates that protein secondary interactions directly influence the relative stabilization/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.</AbstractText>
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