Structural and functional characterization of the hydrogenase-maturation HydF protein

Caserta, Giorgio, Pecqueur, Ludovic, Adamska-Venkatesh, Agnieszka, Papini, Cecilia, Roy, Souvik, Artero, Vincent, Atta, Mohamed, Reijerse, Edward, Lubitz, Wolfgang and Fontecave, Marc (2017) Structural and functional characterization of the hydrogenase-maturation HydF protein. Nature Chemical Biology, 13 (7). pp. 779-784. ISSN 1552-4450

Full content URL: https://doi.org/10.1038/nchembio.2385

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Item Type:Article
Item Status:Live Archive

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.

Keywords:Bioinorganic chemistry, Chemical modification, Enzymes, x-ray crystallography
Subjects:C Biological Sciences > C720 Biological Chemistry
F Physical Sciences > F100 Chemistry
F Physical Sciences > F163 Bio-organic Chemistry
Divisions:College of Science > School of Chemistry
ID Code:40667
Deposited On:17 Apr 2020 12:11

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