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

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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Main Authors: Joseph M. Pennington, Michael Kemp, Lauren McGarry, Yu Chen, M. Elizabeth Stroupe
Format: Article
Language:English
Published: Nature Publishing Group 2020-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-14722-1
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spelling doaj-ea8b31747188498a8b3a178dfb2ba7c02021-05-11T08:37:30ZengNature Publishing GroupNature Communications2041-17232020-02-0111111110.1038/s41467-020-14722-1Siroheme synthase orients substrates for dehydrogenase and chelatase activities in a common active siteJoseph M. Pennington0Michael Kemp1Lauren McGarry2Yu Chen3M. Elizabeth Stroupe4Department of Biological Science and Institute of Molecular Biophysics, Florida State UniversityDepartment of Molecular Medicine, University of South Florida College of MedicineDepartment of Biological Science and Institute of Molecular Biophysics, Florida State UniversityDepartment of Molecular Medicine, University of South Florida College of MedicineDepartment of Biological Science and Institute of Molecular Biophysics, Florida State UniversitySiroheme 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.https://doi.org/10.1038/s41467-020-14722-1
collection DOAJ
language English
format Article
sources DOAJ
author Joseph M. Pennington
Michael Kemp
Lauren McGarry
Yu Chen
M. Elizabeth Stroupe
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2020-02-01
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.
url https://doi.org/10.1038/s41467-020-14722-1
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