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Reversible 4Fe-3S cluster morphing in an O2-tolerant NiFe hydrogenase
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Reversible 4Fe-3S cluster morphing in an O2-tolerant NiFe hydrogenase
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Journal Article
Reversible 4Fe-3S cluster morphing in an O2-tolerant NiFe hydrogenase
2014
Overview
Certain oxygen-tolerant hydrogenases contain a unique [4Fe-3S] cluster near the catalytic site, but the role of this cofactor is not fully understood. Crystallographic, spectroscopic and computational data now provide evidence for redox-dependent transformations of this cluster, potentially explaining how specialized hydrogenases can safely reduce inhibitory O
2
.
Hydrogenases catalyze the reversible oxidation of H
2
into protons and electrons and are usually readily inactivated by O
2
. However, a subgroup of the [NiFe] hydrogenases, including the membrane-bound [NiFe] hydrogenase from
Ralstonia eutropha,
has evolved remarkable tolerance toward O
2
that enables their host organisms to utilize H
2
as an energy source at high O
2
. This feature is crucially based on a unique six cysteine-coordinated [4Fe-3S] cluster located close to the catalytic center, whose properties were investigated in this study using a multidisciplinary approach. The [4Fe-3S] cluster undergoes redox-dependent reversible transformations, namely iron swapping between a sulfide and a peptide amide N. Moreover, our investigations unraveled the redox-dependent and reversible occurence of an oxygen ligand located at a different iron. This ligand is hydrogen bonded to a conserved histidine that is essential for H
2
oxidation at high O
2
. We propose that these transformations, reminiscent of those of the P-cluster of nitrogenase, enable the consecutive transfer of two electrons within a physiological potential range.
