The influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.

The class of [NiFe]-hydrogenases is characterized by a bimetallic cofactor comprising low-spin nickel and iron ions, the latter of which is modified with a single carbon monoxide (CO) and two cyanide (CN-) molecules. Generation of these ligands in vivo requires a complex maturation apparatus in whic...

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Autores principales:	Sven T Stripp, Ute Lindenstrauss, Claudia Granich, R Gary Sawers, Basem Soboh
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3162823ec6924c919dfea1dafd97752d
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spelling	oai:doaj.org-article:3162823ec6924c919dfea1dafd97752d2021-11-25T06:00:59ZThe influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.1932-620310.1371/journal.pone.0107488https://doaj.org/article/3162823ec6924c919dfea1dafd97752d2014-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0107488https://doaj.org/toc/1932-6203The class of [NiFe]-hydrogenases is characterized by a bimetallic cofactor comprising low-spin nickel and iron ions, the latter of which is modified with a single carbon monoxide (CO) and two cyanide (CN-) molecules. Generation of these ligands in vivo requires a complex maturation apparatus in which the HypC-HypD complex acts as a 'construction site' for the Fe-(CN)2CO portion of the cofactor. The order of addition of the CO and CN- ligands determines the ultimate structure and catalytic efficiency of the cofactor; however much debate surrounds the succession of events. Here, we present an FT-IR spectroscopic analysis of HypC-HypD isolated from a hydrogenase-competent wild-type strain of Escherichia coli. In contrast to previously reported samples, HypC-HypD showed spectral contributions indicative of an electron-rich Fe-CO cofactor, at the same time lacking any Fe-CN- signatures. This immature iron site binds external CO and undergoes oxidative damage when in contact with O2. Binding of CO protects the site against loss of spectral features associated with O2 damage. Our findings strongly suggest that CO ligation precedes cyanation in vivo. Furthermore, the results provide a rationale for the deleterious effects of O2 on in vivo cofactor biosynthesis.Sven T StrippUte LindenstraussClaudia GranichR Gary SawersBasem SobohPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 9, p e107488 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sven T Stripp Ute Lindenstrauss Claudia Granich R Gary Sawers Basem Soboh The influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.
description	The class of [NiFe]-hydrogenases is characterized by a bimetallic cofactor comprising low-spin nickel and iron ions, the latter of which is modified with a single carbon monoxide (CO) and two cyanide (CN-) molecules. Generation of these ligands in vivo requires a complex maturation apparatus in which the HypC-HypD complex acts as a 'construction site' for the Fe-(CN)2CO portion of the cofactor. The order of addition of the CO and CN- ligands determines the ultimate structure and catalytic efficiency of the cofactor; however much debate surrounds the succession of events. Here, we present an FT-IR spectroscopic analysis of HypC-HypD isolated from a hydrogenase-competent wild-type strain of Escherichia coli. In contrast to previously reported samples, HypC-HypD showed spectral contributions indicative of an electron-rich Fe-CO cofactor, at the same time lacking any Fe-CN- signatures. This immature iron site binds external CO and undergoes oxidative damage when in contact with O2. Binding of CO protects the site against loss of spectral features associated with O2 damage. Our findings strongly suggest that CO ligation precedes cyanation in vivo. Furthermore, the results provide a rationale for the deleterious effects of O2 on in vivo cofactor biosynthesis.
format	article
author	Sven T Stripp Ute Lindenstrauss Claudia Granich R Gary Sawers Basem Soboh
author_facet	Sven T Stripp Ute Lindenstrauss Claudia Granich R Gary Sawers Basem Soboh
author_sort	Sven T Stripp
title	The influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.
title_short	The influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.
title_full	The influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.
title_fullStr	The influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.
title_full_unstemmed	The influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.
title_sort	influence of oxygen on [nife]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/3162823ec6924c919dfea1dafd97752d
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The influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.

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