A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state

The diheme enzyme MauG forms a bis-Fe(IV) state. Here the authors identify and determine the structure of BthA, a diheme peroxidase conserved in all Burkholderia and show that BthA also forms a bis-Fe(IV) species but mechanistically differs from MauG by combining magnetic resonance, near-IR and Möss...

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Autores principales:	Kimberly Rizzolo, Steven E. Cohen, Andrew C. Weitz, Madeline M. López Muñoz, Michael P. Hendrich, Catherine L. Drennan, Sean J. Elliott
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/43e89e2788134c44bc04e90574efd768
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spelling	oai:doaj.org-article:43e89e2788134c44bc04e90574efd7682021-12-02T14:38:42ZA widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state10.1038/s41467-019-09020-42041-1723https://doaj.org/article/43e89e2788134c44bc04e90574efd7682019-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-09020-4https://doaj.org/toc/2041-1723The diheme enzyme MauG forms a bis-Fe(IV) state. Here the authors identify and determine the structure of BthA, a diheme peroxidase conserved in all Burkholderia and show that BthA also forms a bis-Fe(IV) species but mechanistically differs from MauG by combining magnetic resonance, near-IR and Mössbauer spectroscopies and electrochemical methods.Kimberly RizzoloSteven E. CohenAndrew C. WeitzMadeline M. López MuñozMichael P. HendrichCatherine L. DrennanSean J. ElliottNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Kimberly Rizzolo Steven E. Cohen Andrew C. Weitz Madeline M. López Muñoz Michael P. Hendrich Catherine L. Drennan Sean J. Elliott A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state
description	The diheme enzyme MauG forms a bis-Fe(IV) state. Here the authors identify and determine the structure of BthA, a diheme peroxidase conserved in all Burkholderia and show that BthA also forms a bis-Fe(IV) species but mechanistically differs from MauG by combining magnetic resonance, near-IR and Mössbauer spectroscopies and electrochemical methods.
format	article
author	Kimberly Rizzolo Steven E. Cohen Andrew C. Weitz Madeline M. López Muñoz Michael P. Hendrich Catherine L. Drennan Sean J. Elliott
author_facet	Kimberly Rizzolo Steven E. Cohen Andrew C. Weitz Madeline M. López Muñoz Michael P. Hendrich Catherine L. Drennan Sean J. Elliott
author_sort	Kimberly Rizzolo
title	A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state
title_short	A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state
title_full	A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state
title_fullStr	A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state
title_full_unstemmed	A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state
title_sort	widely distributed diheme enzyme from burkholderia that displays an atypically stable bis-fe(iv) state
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/43e89e2788134c44bc04e90574efd768
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A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state

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