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Studies on hydrogenase

Hydrogenases are microbial enzymes which catalyze uptake and production of H(2). Hydrogenases are classified into 10 classes based on the electron carrier specificity, or into 3 families, [NiFe]-family (including [NiFeSe]-subfamily), [FeFe]-family and [Fe]-family, based on the metal composition of t...

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Autores principales: YAGI, Tatsuhiko, HIGUCHI, Yoshiki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Japan Academy 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3611953/
https://www.ncbi.nlm.nih.gov/pubmed/23318679
http://dx.doi.org/10.2183/pjab.89.16
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author YAGI, Tatsuhiko
HIGUCHI, Yoshiki
author_facet YAGI, Tatsuhiko
HIGUCHI, Yoshiki
author_sort YAGI, Tatsuhiko
collection PubMed
description Hydrogenases are microbial enzymes which catalyze uptake and production of H(2). Hydrogenases are classified into 10 classes based on the electron carrier specificity, or into 3 families, [NiFe]-family (including [NiFeSe]-subfamily), [FeFe]-family and [Fe]-family, based on the metal composition of the active site. H(2) is heterolytically cleaved on the enzyme (E) to produce EH(a)H(b), where H(a) and H(b) have different rate constants for exchange with the medium hydron. X-ray crystallography unveiled the three-dimensional structures of hydrogenases. The simplest [NiFe]-hydrogenase is a heterodimer, in which the large subunit bears the Ni-Fe center buried deep in the protein, and the small subunit bears iron-sulfur clusters, which mediate electron transfer between the Ni-Fe center and the protein surface. Some hydrogenases have additional subunit(s) for interaction with their electron carriers. Various redox states of the enzyme were characterized by EPR, FTIR, etc. Based on the kinetic, structural and spectroscopic studies, the catalytic mechanism of [NiFe]-hydrogenase was proposed to explain H(2)-uptake, H(2)-production and isotopic exchange reactions.
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spelling pubmed-36119532013-04-11 Studies on hydrogenase YAGI, Tatsuhiko HIGUCHI, Yoshiki Proc Jpn Acad Ser B Phys Biol Sci Review Hydrogenases are microbial enzymes which catalyze uptake and production of H(2). Hydrogenases are classified into 10 classes based on the electron carrier specificity, or into 3 families, [NiFe]-family (including [NiFeSe]-subfamily), [FeFe]-family and [Fe]-family, based on the metal composition of the active site. H(2) is heterolytically cleaved on the enzyme (E) to produce EH(a)H(b), where H(a) and H(b) have different rate constants for exchange with the medium hydron. X-ray crystallography unveiled the three-dimensional structures of hydrogenases. The simplest [NiFe]-hydrogenase is a heterodimer, in which the large subunit bears the Ni-Fe center buried deep in the protein, and the small subunit bears iron-sulfur clusters, which mediate electron transfer between the Ni-Fe center and the protein surface. Some hydrogenases have additional subunit(s) for interaction with their electron carriers. Various redox states of the enzyme were characterized by EPR, FTIR, etc. Based on the kinetic, structural and spectroscopic studies, the catalytic mechanism of [NiFe]-hydrogenase was proposed to explain H(2)-uptake, H(2)-production and isotopic exchange reactions. The Japan Academy 2013-01-11 /pmc/articles/PMC3611953/ /pubmed/23318679 http://dx.doi.org/10.2183/pjab.89.16 Text en © 2013 The Japan Academy This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
YAGI, Tatsuhiko
HIGUCHI, Yoshiki
Studies on hydrogenase
title Studies on hydrogenase
title_full Studies on hydrogenase
title_fullStr Studies on hydrogenase
title_full_unstemmed Studies on hydrogenase
title_short Studies on hydrogenase
title_sort studies on hydrogenase
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3611953/
https://www.ncbi.nlm.nih.gov/pubmed/23318679
http://dx.doi.org/10.2183/pjab.89.16
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