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The Mossbauer parameters of the proximal cluster of membrane-bound hydrogenase revisited: a density functional theory study

Academic Article
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Overview

authors

  • Tabrizi, S. G.
  • Pelmenschikov, V.
  • Noodleman, Louis
  • Kaupp, M.

publication date

  • January 2016

journal

  • Journal of Chemical Theory and Computation  Journal

abstract

  • An unprecedented [4Fe-3S] cluster proximal to the regular [NiFe] active site has recently been found to be responsible for the ability of membrane-bound hydrogenases (MBHs) to oxidize dihydrogen in the presence of ambient levels of oxygen. Starting from proximal cluster models of a recent DFT study on the redox-dependent structural transformation of the [4Fe-3S] cluster, (57)Fe Mössbauer parameters (electric field gradients, isomer shifts, and nuclear hyperfine couplings) were calculated using DFT. Our results revise the previously reported correspondence of Mössbauer signals and iron centers in the [4Fe-3S](3+) reduced-state proximal cluster. Similar conflicting assignments are also resolved for the [4Fe-3S](5+) superoxidized state with particular regard to spin-coupling in the broken-symmetry DFT calculations. Calculated (57)Fe hyperfine coupling (HFC) tensors expose discrepancies in the experimental set of HFC tensors and substantiate the need for additional experimental work on the magnetic properties of the MBH proximal cluster in its reduced and superoxidized redox states.

subject areas

  • Crystallography, X-Ray
  • Electron Spin Resonance Spectroscopy
  • Hydrogenase
  • Iron
  • Iron-Sulfur Proteins
  • Models, Molecular
  • Oxidation-Reduction
  • Oxygen
  • Quantum Theory
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Identity

PubMed Central ID

  • PMC4819768

International Standard Serial Number (ISSN)

  • 1549-9618

Digital Object Identifier (DOI)

  • 10.1021/acs.jctc.5b00854

PubMed ID

  • 26598030
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Additional Document Info

start page

  • 174

volume

  • 12

issue

  • 1

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