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

Willistein, M., Bechtel, D. F., Müller, C. S., Demmer, U., Heimann, L., Kayastha, K., et al. (2019). Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactorsLow potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors. Nature Communications, 10: 2074. doi:10.1038/s41467-019-10078-3.

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 Creators:
Willistein, Max1, Author
Bechtel, Dominique F.2, Author
Müller, Christina S.3, Author
Demmer, Ulrike4, Author              
Heimann, Larissa3, Author
Kayastha, Kanwal4, Author              
Schünemann, Volker3, Author
Pierik, Antonio J.2, Author
Ullmann, G. Matthias5, Author
Ermler, Ulrich4, Author              
Boll, Matthias1, Author
Affiliations:
1Microbiology, Faculty of Biology, University of Freiburg, Schänzlestrasse 1, 79104, Freiburg, Germany, ou_persistent22              
2Biochemistry, Faculty of Chemistry, University of Kaiserslautern, Erwin-Schrödinger-Straße 52, 67663, Kaiserslautern, Germany, ou_persistent22              
3Biophysics, Department of Physics, University of Kaiserslautern, Erwin-Schrödinger-Straße 46, 67663, Kaiserslautern, Germany, ou_persistent22              
4Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
5Computational Biochemistry, University of Bayreuth, Universitätsstrasse 30, NW I, 95447, Bayreuth, Germany, ou_persistent22              

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Language(s): eng - English
 Dates: 2019-01-252019-04-122019-05-06
 Publication Status: Published online
 Pages: 10
 Publishing info: -
 Table of Contents: Hydride transfers play a crucial role in a multitude of biological redox reactions and are mediated by flavin, deazaflavin or nicotinamide adenine dinucleotide cofactors at standard redox potentials ranging from 0 to –340 mV. 2-Naphthoyl-CoA reductase, a key enzyme of oxygen-independent bacterial naphthalene degradation, uses a low-potential one-electron donor for the two-electron dearomatization of its substrate below the redox limit of known biological hydride transfer processes at E°’ = −493 mV. Here we demonstrate by X-ray structural analyses, QM/MM computational studies, and multiple spectroscopy/activity based titrations that highly cooperative electron transfer (n = 3) from a low-potential one-electron (FAD) to a two-electron (FMN) transferring flavin cofactor is the key to overcome the resonance stabilized aromatic system by hydride transfer in a highly hydrophobic pocket. The results evidence how the protein environment inversely functionalizes two flavins to switch from low-potential one-electron to hydride transfer at the thermodynamic limit of flavin redox chemistry
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-019-10078-3
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 10 Sequence Number: 2074 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723