Stepwise conversion of the Cys6[4Fe–3S] to a Cys4[4Fe–4S] cluster and its impact on the oxygen tolerance of [NiFe]-hydrogenase

Author:

Schmidt Andrea1,Kalms Jacqueline1,Lorent Christian2ORCID,Katz Sagie2,Frielingsdorf Stefan2ORCID,Evans Rhiannon M.3ORCID,Fritsch Johannes2,Siebert Elisabeth2,Teutloff Christian4,Armstrong Fraser A.3ORCID,Zebger Ingo2ORCID,Lenz Oliver2ORCID,Scheerer Patrick1ORCID

Affiliation:

1. Charité – Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Institute of Medical Physics and Biophysics (CC2), Group Structural Biology of Cellular Signaling, Charitéplatz 1, 10117 Berlin, Germany

2. Institut für Chemie, Biophysical Chemistry, Technische Universität Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany

3. Department of Chemistry, University of Oxford, OX1 3QR Oxford, UK

4. Department of Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany

Abstract

The [4Fe-3S] cluster of an O2-tolerant [NiFe] hydrogenase was transformed into different [4Fe-4S] clusters, and structural, spectroscopic and electrochemical analyses of the enzyme variants revealed an O2-tolerance mechanism at various levels.

Funder

Deutsche Forschungsgemeinschaft

Biotechnology and Biological Sciences Research Council

Einstein Stiftung Berlin

Horizon 2020 Framework Programme

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

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