Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site

Siroheme is an essential bacterial iron tetrapyrrole used by siroheme-dependent sulfite and nitrite reductases. Here the authors shed light on the catalytic mechanisms of siroheme synthase through the structures of the bifunctional dehydrogenase/chelatase CysG module bound to its substrate, precorri...

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Autores principales:	Joseph M. Pennington, Michael Kemp, Lauren McGarry, Yu Chen, M. Elizabeth Stroupe
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ea8b31747188498a8b3a178dfb2ba7c0
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spelling	oai:doaj.org-article:ea8b31747188498a8b3a178dfb2ba7c02021-12-02T15:39:17ZSiroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site10.1038/s41467-020-14722-12041-1723https://doaj.org/article/ea8b31747188498a8b3a178dfb2ba7c02020-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14722-1https://doaj.org/toc/2041-1723Siroheme is an essential bacterial iron tetrapyrrole used by siroheme-dependent sulfite and nitrite reductases. Here the authors shed light on the catalytic mechanisms of siroheme synthase through the structures of the bifunctional dehydrogenase/chelatase CysG module bound to its substrate, precorrin-2, the product/substrate sirohydrochlorin, and cobalt-sirohydrochlorin.Joseph M. PenningtonMichael KempLauren McGarryYu ChenM. Elizabeth StroupeNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Joseph M. Pennington Michael Kemp Lauren McGarry Yu Chen M. Elizabeth Stroupe Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site
description	Siroheme is an essential bacterial iron tetrapyrrole used by siroheme-dependent sulfite and nitrite reductases. Here the authors shed light on the catalytic mechanisms of siroheme synthase through the structures of the bifunctional dehydrogenase/chelatase CysG module bound to its substrate, precorrin-2, the product/substrate sirohydrochlorin, and cobalt-sirohydrochlorin.
format	article
author	Joseph M. Pennington Michael Kemp Lauren McGarry Yu Chen M. Elizabeth Stroupe
author_facet	Joseph M. Pennington Michael Kemp Lauren McGarry Yu Chen M. Elizabeth Stroupe
author_sort	Joseph M. Pennington
title	Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site
title_short	Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site
title_full	Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site
title_fullStr	Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site
title_full_unstemmed	Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site
title_sort	siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/ea8b31747188498a8b3a178dfb2ba7c0
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Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active site

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