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

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Demmer,  Julius K.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Rupprecht,  Fiona A.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Department of Synaptic Plasticity, Max Planck Institute for Brain Research, Frankfurt am Main, Max Planck Society;

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Eisinger,  Martin L.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Ermler,  Ulrich       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Langer,  Julian David       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Department of Synaptic Plasticity, Max Planck Institute for Brain Research, Frankfurt am Main, Max Planck Society;

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Citation

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.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-1D01-7
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.