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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
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Functional Dynamics of an Ancient Membrane-Bound Hydrogenase
Max E Mühlbauer1,2, Ana P Gamiz-Hernandez1, Ville R I Kaila1,2
1Department of Biochemistry and Biophysics, Stockholm University, 10691 Stockholm, Sweden.
Journal of the American Chemical Society
|November 30, 2021
Summary
Membrane-bound hydrogenase (Mbh) uses hydrogen gas energy to pump ions across archaeal membranes. This study reveals how ion binding and protonation changes drive this crucial bioenergetic process.
Area of Science:
- Biochemistry
- Molecular Biology
- Bioenergetics
Background:
- The membrane-bound hydrogenase (Mbh) is a crucial redox-driven Na+/H+ transporter in archaea.
- Understanding its ion transport mechanism is key to comprehending early cellular bioenergetics.
Purpose of the Study:
- To elucidate the molecular principles of proton and sodium transport in Mbh from *Pyrococcus furiosus*.
- To investigate the coupling mechanisms between ion binding, protonation, and conformational changes.
Main Methods:
- Atomistic molecular dynamics (MD) simulations.
- Data clustering methods.
- Quantum chemical calculations.
Main Results:
- Identified putative Na+ binding sites and proton pathways.
- Revealed conformational changes regulating ion uptake.
- Suggested coupling between Na+ binding/protonation and proton transfer via conserved ion pairs.
Conclusions:
- Provided functional insight into archaeal energy transduction.
- Illustrated conserved coupling principles within the complex I superfamily.
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