Structural and functional characterization of the hydrogenase-maturation HydF protein Article - 2017

Giorgio Caserta, Ludovic Pecqueur, Agnieszka Adamska-Venkatesh, Cécilia Papini, Souvik Roy, Vincent Artero, Mohamed Atta, Edward Reijerse, Wolfgang Lubitz, Marc Fontecave

Giorgio Caserta, Ludovic Pecqueur, Agnieszka Adamska-Venkatesh, Cécilia Papini, Souvik Roy, Vincent Artero, Mohamed Atta, Edward Reijerse, Wolfgang Lubitz, Marc Fontecave, « Structural and functional characterization of the hydrogenase-maturation HydF protein  », Nature Chemical Biology, 2017, pp. 779-784. ISSN 1552-4450

Abstract

[FeFe] hydrogenase (HydA) catalyzes interconversion between 2H+ and H2 at an active site composed of a [4Fe-4S] cluster linked to a 2Fe subcluster that harbors CO, CN− and azapropanedithiolate (adt2−) 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. [Fe2(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.

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