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  Ligand binding and conformational dynamics in a flavin-based electron-bifurcating enzyme complex revealed by Hydrogen-Deuterium Exchange Mass Spectrometry

Demmer, J. K., Rupprecht, F. A., Eisinger, M. L., Ermler, U., & Langer, J. D. (2016). Ligand binding and conformational dynamics in a flavin-based electron-bifurcating enzyme complex revealed by Hydrogen-Deuterium Exchange Mass Spectrometry. FEBS Letters, 590(24), 4472-4479. doi:10.1002/1873-3468.12489.

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 Creators:
Demmer, Julius K.1, Author           
Rupprecht, Fiona A.1, 2, Author           
Eisinger, Martin L.1, Author           
Ermler, Ulrich1, Author                 
Langer, Julian David1, 2, Author                 
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Department of Synaptic Plasticity, Max Planck Institute for Brain Research, Frankfurt am Main, Max Planck Society, ou_persistent22              

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Free keywords: flavin-based electron bifurcation; Hydrogen–Deuterium Exchange Mass Spectrometry
 Abstract: Flavin-based electron bifurcation (FBEB) is a novel mechanism of energy coupling used by anaerobic microorganisms to optimize their energy metabolism efficiency. The first high-resolution structure of a complete FBEB enzyme complex, the NADH-dependent reduced ferredoxin: NADP+-oxidoreductase (NfnAB) of Thermotoga maritima, was recently solved. However, no experimental evidence for the NADPH-binding site and conformational changes during the FBEB reaction are available. Here we analyzed ligand binding and the conformational dynamics of oxygen-sensitive NfnAB using Hydrogen–Deuterium Exchange Mass-Spectrometry, including a customized anaerobic workflow. We confirmed the NADH and the previously postulated NADPH-binding site. Furthermore, we observed an NfnA-NfnB rearrangement upon NADPH binding which supports the proposed FBEB mechanism.

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Language(s): eng - English
 Dates: 2016-10-052016-11-142016-12-162016-12
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/1873-3468.12489
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 590 (24) Sequence Number: - Start / End Page: 4472 - 4479 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501