Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors

The reduction of 2-naphtoyl-CoA to 5,6 dihydro-2-naphtoyl-CoA by 2-naphtoyl-CoA reductase is below the negative redox limit usually encountered in biological hydride transfer. Here, via X-ray crystallography and spectroscopic analysis, the authors elucidated the mechanism behind this.

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Autores principales: Max Willistein, Dominique F. Bechtel, Christina S. Müller, Ulrike Demmer, Larissa Heimann, Kanwal Kayastha, Volker Schünemann, Antonio J. Pierik, G. Matthias Ullmann, Ulrich Ermler, Matthias Boll
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Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/5384fcc9585141cc8574aa70b0d76cdc
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spelling oai:doaj.org-article:5384fcc9585141cc8574aa70b0d76cdc2021-12-02T14:38:39ZLow potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors10.1038/s41467-019-10078-32041-1723https://doaj.org/article/5384fcc9585141cc8574aa70b0d76cdc2019-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10078-3https://doaj.org/toc/2041-1723The reduction of 2-naphtoyl-CoA to 5,6 dihydro-2-naphtoyl-CoA by 2-naphtoyl-CoA reductase is below the negative redox limit usually encountered in biological hydride transfer. Here, via X-ray crystallography and spectroscopic analysis, the authors elucidated the mechanism behind this.Max WillisteinDominique F. BechtelChristina S. MüllerUlrike DemmerLarissa HeimannKanwal KayasthaVolker SchünemannAntonio J. PierikG. Matthias UllmannUlrich ErmlerMatthias BollNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Max Willistein
Dominique F. Bechtel
Christina S. Müller
Ulrike Demmer
Larissa Heimann
Kanwal Kayastha
Volker Schünemann
Antonio J. Pierik
G. Matthias Ullmann
Ulrich Ermler
Matthias Boll
Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors
description The reduction of 2-naphtoyl-CoA to 5,6 dihydro-2-naphtoyl-CoA by 2-naphtoyl-CoA reductase is below the negative redox limit usually encountered in biological hydride transfer. Here, via X-ray crystallography and spectroscopic analysis, the authors elucidated the mechanism behind this.
format article
author Max Willistein
Dominique F. Bechtel
Christina S. Müller
Ulrike Demmer
Larissa Heimann
Kanwal Kayastha
Volker Schünemann
Antonio J. Pierik
G. Matthias Ullmann
Ulrich Ermler
Matthias Boll
author_facet Max Willistein
Dominique F. Bechtel
Christina S. Müller
Ulrike Demmer
Larissa Heimann
Kanwal Kayastha
Volker Schünemann
Antonio J. Pierik
G. Matthias Ullmann
Ulrich Ermler
Matthias Boll
author_sort Max Willistein
title Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors
title_short Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors
title_full Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors
title_fullStr Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors
title_full_unstemmed Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors
title_sort low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/5384fcc9585141cc8574aa70b0d76cdc
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