Homologous bd oxidases share the same architecture but differ in mechanism

Cytochrome bd oxidases couple quinol oxidation and the release of protons to the periplasmic side with proton uptake from the cytoplasmic side to reduce dioxygen to water and they are the terminal reductases in bacterial and archaeal respiratory chains. Here the authors present the cryo-EM structure...

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Autores principales:	Alexander Theßeling, Tim Rasmussen, Sabrina Burschel, Daniel Wohlwend, Jan Kägi, Rolf Müller, Bettina Böttcher, Thorsten Friedrich
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/380da862893749fc97e0898f2e736f22
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spelling	oai:doaj.org-article:380da862893749fc97e0898f2e736f222021-12-02T17:01:26ZHomologous bd oxidases share the same architecture but differ in mechanism10.1038/s41467-019-13122-42041-1723https://doaj.org/article/380da862893749fc97e0898f2e736f222019-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13122-4https://doaj.org/toc/2041-1723Cytochrome bd oxidases couple quinol oxidation and the release of protons to the periplasmic side with proton uptake from the cytoplasmic side to reduce dioxygen to water and they are the terminal reductases in bacterial and archaeal respiratory chains. Here the authors present the cryo-EM structure of Escherichia coli bd oxidase and discuss mechanistic implications.Alexander TheßelingTim RasmussenSabrina BurschelDaniel WohlwendJan KägiRolf MüllerBettina BöttcherThorsten FriedrichNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-7 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Alexander Theßeling Tim Rasmussen Sabrina Burschel Daniel Wohlwend Jan Kägi Rolf Müller Bettina Böttcher Thorsten Friedrich Homologous bd oxidases share the same architecture but differ in mechanism
description	Cytochrome bd oxidases couple quinol oxidation and the release of protons to the periplasmic side with proton uptake from the cytoplasmic side to reduce dioxygen to water and they are the terminal reductases in bacterial and archaeal respiratory chains. Here the authors present the cryo-EM structure of Escherichia coli bd oxidase and discuss mechanistic implications.
format	article
author	Alexander Theßeling Tim Rasmussen Sabrina Burschel Daniel Wohlwend Jan Kägi Rolf Müller Bettina Böttcher Thorsten Friedrich
author_facet	Alexander Theßeling Tim Rasmussen Sabrina Burschel Daniel Wohlwend Jan Kägi Rolf Müller Bettina Böttcher Thorsten Friedrich
author_sort	Alexander Theßeling
title	Homologous bd oxidases share the same architecture but differ in mechanism
title_short	Homologous bd oxidases share the same architecture but differ in mechanism
title_full	Homologous bd oxidases share the same architecture but differ in mechanism
title_fullStr	Homologous bd oxidases share the same architecture but differ in mechanism
title_full_unstemmed	Homologous bd oxidases share the same architecture but differ in mechanism
title_sort	homologous bd oxidases share the same architecture but differ in mechanism
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/380da862893749fc97e0898f2e736f22
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Homologous bd oxidases share the same architecture but differ in mechanism

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