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Journal Article

His-Ligation to the [4Fe-4S] Subcluster Tunes the Catalytic Bias of [FeFe] Hydrogenase

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Rodriguez-Macia,  Patricia
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Birrell,  James A.
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Lubitz,  Wolfgang
Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Rüdiger,  Olaf
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Citation

Rodriguez-Macia, P., Kertess, L., Burnik, J., Birrell, J. A., Hofmann, E., Lubitz, W., et al. (2019). His-Ligation to the [4Fe-4S] Subcluster Tunes the Catalytic Bias of [FeFe] Hydrogenase. The Journal of Organic Chemistry, 141(1), 472-481. doi:10.1021/jacs.8b11149.


Cite as: https://hdl.handle.net/21.11116/0000-0006-5D83-E
Abstract
[FeFe] hydrogenases interconvert H-2 into protons and electrons reversibly and efficiently. The active site H-cluster is composed of two sites: a unique [2Fe] subcluster ([2Fe](H)) covalently linked via cysteine to a canonical [4Fe-4S] cluster ([4Fe-4S](H)). Both sites are redox active and electron transfer is proton-coupled, such that the potential of the H-cluster lies very close to the H-2 thermodynamic potential, which confers the enzyme with the ability to operate quickly in both directions without energy losses. Here, one of the cysteines coordinating [4Fe-4S](H) (Cys362) in the [FeFe] hydrogenase from the green algae Chlamydomonas reinhardtii (CrHydAl) was exchanged with histidine and the resulting C362H variant was shown to contain a [4Fe-4S] cluster with a more positive redox potential than the wild-type. The change in the [4Fe-4S] cluster potential resulted in a shift of the catalytic bias, diminishing the H-2 production activity but giving significantly higher H-2 oxidation activity, albeit with a 200 mV overpotential requirement. These results highlight the importance of the [4Fe-4S] cluster as an electron injection site, modulating the redox potential and the catalytic properties of the H-cluster.