Reversible [4Fe-3S] cluster morphing in an O(2)-tolerant [NiFe] hydrogenase

Stefan Frielingsdorf1, Johannes Fritsch2, Andrea Schmidt3

  • 11] Institut für Biologie-Mikrobiologie, Humboldt-Universität zu Berlin, Berlin, Germany. [2] Institut für Chemie, Sekr. PC14, Technische Universität Berlin, Berlin, Germany.

Summary

Certain [NiFe] hydrogenases resist oxygen damage, allowing hydrogen utilization in aerobic environments. This resilience stems from a unique [4Fe-3S] cluster that undergoes redox-dependent transformations, facilitating electron transfer.

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