An evolutionary path to altered cofactor specificity in a metalloenzyme

Many metalloenzymes are highly specific for their cognate metal ion but the molecular principles underlying this specificity often remain unclear. Here, the authors characterize the structural and biochemical basis for the different metal specificity of two evolutionarily related superoxide dismutas...

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Autores principales:	Anna Barwinska-Sendra, Yuritzi M. Garcia, Kacper M. Sendra, Arnaud Baslé, Eilidh S. Mackenzie, Emma Tarrant, Patrick Card, Leandro C. Tabares, Cédric Bicep, Sun Un, Thomas E. Kehl-Fie, Kevin J. Waldron
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6c637b09e75b4404830df194ffd54159
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spelling	oai:doaj.org-article:6c637b09e75b4404830df194ffd541592021-12-02T18:24:58ZAn evolutionary path to altered cofactor specificity in a metalloenzyme10.1038/s41467-020-16478-02041-1723https://doaj.org/article/6c637b09e75b4404830df194ffd541592020-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16478-0https://doaj.org/toc/2041-1723Many metalloenzymes are highly specific for their cognate metal ion but the molecular principles underlying this specificity often remain unclear. Here, the authors characterize the structural and biochemical basis for the different metal specificity of two evolutionarily related superoxide dismutases.Anna Barwinska-SendraYuritzi M. GarciaKacper M. SendraArnaud BasléEilidh S. MackenzieEmma TarrantPatrick CardLeandro C. TabaresCédric BicepSun UnThomas E. Kehl-FieKevin J. WaldronNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Anna Barwinska-Sendra Yuritzi M. Garcia Kacper M. Sendra Arnaud Baslé Eilidh S. Mackenzie Emma Tarrant Patrick Card Leandro C. Tabares Cédric Bicep Sun Un Thomas E. Kehl-Fie Kevin J. Waldron An evolutionary path to altered cofactor specificity in a metalloenzyme
description	Many metalloenzymes are highly specific for their cognate metal ion but the molecular principles underlying this specificity often remain unclear. Here, the authors characterize the structural and biochemical basis for the different metal specificity of two evolutionarily related superoxide dismutases.
format	article
author	Anna Barwinska-Sendra Yuritzi M. Garcia Kacper M. Sendra Arnaud Baslé Eilidh S. Mackenzie Emma Tarrant Patrick Card Leandro C. Tabares Cédric Bicep Sun Un Thomas E. Kehl-Fie Kevin J. Waldron
author_facet	Anna Barwinska-Sendra Yuritzi M. Garcia Kacper M. Sendra Arnaud Baslé Eilidh S. Mackenzie Emma Tarrant Patrick Card Leandro C. Tabares Cédric Bicep Sun Un Thomas E. Kehl-Fie Kevin J. Waldron
author_sort	Anna Barwinska-Sendra
title	An evolutionary path to altered cofactor specificity in a metalloenzyme
title_short	An evolutionary path to altered cofactor specificity in a metalloenzyme
title_full	An evolutionary path to altered cofactor specificity in a metalloenzyme
title_fullStr	An evolutionary path to altered cofactor specificity in a metalloenzyme
title_full_unstemmed	An evolutionary path to altered cofactor specificity in a metalloenzyme
title_sort	evolutionary path to altered cofactor specificity in a metalloenzyme
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/6c637b09e75b4404830df194ffd54159
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An evolutionary path to altered cofactor specificity in a metalloenzyme

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