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Structural and functional characterization of the hydrogenase-maturation HydF protein

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Adamska-Venkatesh,  Agnieszka
Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

Reijerse,  Edward
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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Citation

Caserta, G., Pecqueur, L., Adamska-Venkatesh, A., Papini, C., Roy, S., Artero, V., et al. (2017). Structural and functional characterization of the hydrogenase-maturation HydF protein. Nature Chemical Biology, 13(7), 779-784. doi:10.1038/nchembio.2385.


Cite as: http://hdl.handle.net/21.11116/0000-0006-E1B0-4
Abstract
[FeFe] hydrogenase (HydA) catalyzes interconversion between 2H(+) and H-2 at an active site composed of a [4Fe-4S] cluster linked to a 2Fe subcluster that harbors CO, CN- and azapropanedithiolate (adt(2-)) ligands. HydE, HydG and HydF are the maturases specifically involved in the biosynthesis of the 2Fe subcluster. Using ligands synthesized by HydE and HydG, HydF assembles a di-iron precursor of the 2Fe subcluster and transfers it to HydA for maturation. Here we report the first X-ray structure of HydF with its [4Fe-4S] cluster. The cluster is chelated by three cysteines and an exchangeable glutamate, which allows the binding of synthetic mimics of the 2Fe subcluster. [Fe-2(adt)(CO)(4)(CN)(2)](2-) is proposed to be the true di-iron precursor because, when bound to HydF, it matures HydA and displays features in Fourier transform infrared (FTIR) spectra that are similar to those of the native HydF active intermediate. A new route toward the generation of artificial hydrogenases, as combinations of HydF and such biomimetic complexes, is proposed on the basis of the observed hydrogenase activity of chemically modified HydF.