Spectroscopic and electrochemical characterization of the [NiFeSe] hydrogenase from Desulfovibrio vulgaris Miyazaki F: reversible redox behavior and interactions between electron transfer centers

Jana Riethausen; Olaf Rüdiger; Wolfgang Gärtner; Wolfgang Lubitz; Hannah S Shafaat

doi:10.1002/cbic.201300120

Spectroscopic and electrochemical characterization of the [NiFeSe] hydrogenase from Desulfovibrio vulgaris Miyazaki F: reversible redox behavior and interactions between electron transfer centers

Chembiochem. 2013 Sep 23;14(14):1714-9. doi: 10.1002/cbic.201300120. Epub 2013 Sep 3.

Authors

Jana Riethausen¹, Olaf Rüdiger, Wolfgang Gärtner, Wolfgang Lubitz, Hannah S Shafaat

Affiliation

¹ Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, Muelheim an der Ruhr 45470 (Germany).

PMID: 24038675
DOI: 10.1002/cbic.201300120

Abstract

Characterizing a new hydrogenase: The newly isolated [NiFeSe] hydrogenase from Desulfovibrio vulgaris Miyazaki F displays catalytic properties distinct from other hydrogenase proteins. Here we apply site-specific spectroscopic and electrochemical techniques to characterize these unique features at the molecular level.

Keywords: electrochemistry; hydrogenase; iron-sulfur clusters; selenium; selenocysteine; spectroscopy.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Desulfovibrio vulgaris / enzymology*
Electrochemical Techniques
Electron Spin Resonance Spectroscopy
Electron Transport
Electrons
Hydrogenase / chemistry*
Hydrogenase / metabolism
Oxidation-Reduction
Spectroscopy, Fourier Transform Infrared
Temperature

Substances

nickel-iron-selenium hydrogenase
Hydrogenase