Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases

[FeFe]-hydrogenases catalyze H2-evolution and -oxidation at very high turnover-rates. Here the authors provide experimental evidence for the proposed proton-transfer (PT) pathway by kinetically, spectroscopically, and crystallographically characterizing eleven mutants from the two [FeFe]-hydrogenase...

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Autores principales:	Jifu Duan, Moritz Senger, Julian Esselborn, Vera Engelbrecht, Florian Wittkamp, Ulf-Peter Apfel, Eckhard Hofmann, Sven T. Stripp, Thomas Happe, Martin Winkler
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/4bada01f9d834987b23d9982e7b4807b
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spelling	oai:doaj.org-article:4bada01f9d834987b23d9982e7b4807b2021-12-02T14:38:50ZCrystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases10.1038/s41467-018-07140-x2041-1723https://doaj.org/article/4bada01f9d834987b23d9982e7b4807b2018-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07140-xhttps://doaj.org/toc/2041-1723[FeFe]-hydrogenases catalyze H2-evolution and -oxidation at very high turnover-rates. Here the authors provide experimental evidence for the proposed proton-transfer (PT) pathway by kinetically, spectroscopically, and crystallographically characterizing eleven mutants from the two [FeFe]-hydrogenases CpI and HydA1.Jifu DuanMoritz SengerJulian EsselbornVera EngelbrechtFlorian WittkampUlf-Peter ApfelEckhard HofmannSven T. StrippThomas HappeMartin WinklerNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jifu Duan Moritz Senger Julian Esselborn Vera Engelbrecht Florian Wittkamp Ulf-Peter Apfel Eckhard Hofmann Sven T. Stripp Thomas Happe Martin Winkler Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases
description	[FeFe]-hydrogenases catalyze H2-evolution and -oxidation at very high turnover-rates. Here the authors provide experimental evidence for the proposed proton-transfer (PT) pathway by kinetically, spectroscopically, and crystallographically characterizing eleven mutants from the two [FeFe]-hydrogenases CpI and HydA1.
format	article
author	Jifu Duan Moritz Senger Julian Esselborn Vera Engelbrecht Florian Wittkamp Ulf-Peter Apfel Eckhard Hofmann Sven T. Stripp Thomas Happe Martin Winkler
author_facet	Jifu Duan Moritz Senger Julian Esselborn Vera Engelbrecht Florian Wittkamp Ulf-Peter Apfel Eckhard Hofmann Sven T. Stripp Thomas Happe Martin Winkler
author_sort	Jifu Duan
title	Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases
title_short	Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases
title_full	Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases
title_fullStr	Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases
title_full_unstemmed	Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases
title_sort	crystallographic and spectroscopic assignment of the proton transfer pathway in [fefe]-hydrogenases
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/4bada01f9d834987b23d9982e7b4807b
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_version_	1718390831150268416

Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases

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