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.
Guardado en:
Autores principales: | , , , , , , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/5384fcc9585141cc8574aa70b0d76cdc |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:5384fcc9585141cc8574aa70b0d76cdc |
---|---|
record_format |
dspace |
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 |
work_keys_str_mv |
AT maxwillistein lowpotentialenzymatichydridetransferviahighlycooperativeandinverselyfunctionalizedflavincofactors AT dominiquefbechtel lowpotentialenzymatichydridetransferviahighlycooperativeandinverselyfunctionalizedflavincofactors AT christinasmuller lowpotentialenzymatichydridetransferviahighlycooperativeandinverselyfunctionalizedflavincofactors AT ulrikedemmer lowpotentialenzymatichydridetransferviahighlycooperativeandinverselyfunctionalizedflavincofactors AT larissaheimann lowpotentialenzymatichydridetransferviahighlycooperativeandinverselyfunctionalizedflavincofactors AT kanwalkayastha lowpotentialenzymatichydridetransferviahighlycooperativeandinverselyfunctionalizedflavincofactors AT volkerschunemann lowpotentialenzymatichydridetransferviahighlycooperativeandinverselyfunctionalizedflavincofactors AT antoniojpierik lowpotentialenzymatichydridetransferviahighlycooperativeandinverselyfunctionalizedflavincofactors AT gmatthiasullmann lowpotentialenzymatichydridetransferviahighlycooperativeandinverselyfunctionalizedflavincofactors AT ulrichermler lowpotentialenzymatichydridetransferviahighlycooperativeandinverselyfunctionalizedflavincofactors AT matthiasboll lowpotentialenzymatichydridetransferviahighlycooperativeandinverselyfunctionalizedflavincofactors |
_version_ |
1718390894076362752 |