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dc.contributor.authorPeters, John W.
dc.contributor.authorSchut, Gerrit J.
dc.contributor.authorBoyd, Eric S.
dc.contributor.authorMulder, David W.
dc.contributor.authorShepard, Eric M.
dc.contributor.authorBroderick, Joan B.
dc.contributor.authorKing, Paul W.
dc.contributor.authorAdams, Michael W. W.
dc.identifier.citationPeters, John W., Gerrit J. Schut, Eric S. Boyd, David W. Mulder, Eric M. Shepard, Joan B. Broderick, Paul W. King, and Michael W. W. Adams. [FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation. Biochimica et Biophysica Acta. .
dc.description.abstractThe [FeFe]- and [NiFe]-hydrogenases catalyze the formal interconversion between hydrogen and protons and electrons, possess characteristic non-protein ligands at their catalytic sites and thus share common mechanistic features. Despite the similarities between these two types of hydrogenases, they clearly have distinct evolutionary origins and likely emerged from different selective pressures. [FeFe]-hydrogenases are widely distributed in fermentative anaerobic microorganisms and likely evolved under selective pressure to couple hydrogen production to the recycling of electron carriers that accumulate during anaerobic metabolism. In contrast, many [NiFe]-hydrogenases catalyze hydrogen oxidation as part of energy metabolism and were likely key enzymes in early life and arguably represent the predecessors of modern respiratory metabolism. Although the reversible combination of protons and electrons to generate hydrogen gas is the simplest of chemical reactions, the [FeFe]- and [NiFe]-hydrogenases have distinct mechanisms and differ in the fundamental chemistry associated with proton transfer and control of electron flow that also help to define catalytic bias. A unifying feature of these enzymes is that hydrogen activation itself has been restricted to one solution involving diatomic ligands (carbon monoxide and cyanide) bound to an Fe ion. On the other hand, and quite remarkably, the biosynthetic mechanisms to produce these ligands are exclusive to each type of enzyme. Furthermore, these mechanisms represent two independent solutions to the formation of complex bioinorganic active sites for catalyzing the simplest of chemical reactions, reversible hydrogen oxidation. As such, the [FeFe]- and [NiFe]-hydrogenases are arguably the most profound case of convergent evolution. This article is part of a Special Issue entitled: Fe/S proteins: Analysis, structure, function, biogenesis and diseases.en_US
dc.title[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturationen_US
mus.citation.journaltitleBiochimica et Biophysica Acta - Molecular Cell Researchen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.collegeCollege of Letters & Science
mus.relation.departmentMicrobiology & Immunology.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.contributor.orcidBroderick, Joan B.|0000-0001-7057-9124en_US
mus.contributor.orcidPeters, John W.|0000-0001-9117-9568en_US

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