The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN- ligated iron cofactor.

Abstract

Biosynthesis of the [FeFe] hydrogenases active site (H-cluster) requires three maturation factors whose respective roles are not understood yet. The clostridial maturation enzymes (CaHydE, CaHydF and CaHydG) were homologously overexpressed in their native host Clostridium acetobutylicum. CaHydF was able to activate Chlamydomonas reinhardtii [FeFe] hydrogenase apoprotein (CrHydA1(apo)) to almost 100% compared to the native specific hydrogen evolution activity. Based on electron paramagnetic resonance spectroscopy and Fourier-transform infrared spectroscopy data the existence of a [4Fe4S] cluster and a CO and CN(-) ligand coordinated di-iron cluster is suggested. This study contains the first experimental evidence that the bi-nuclear part of the H-cluster is assembled in HydF.

DOI: 10.1016/j.febslet.2009.12.016

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@article{Czech2010TheM, title={The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN- ligated iron cofactor.}, author={Ilka Czech and Alexey Silakov and Wolfgang Lubitz and Thomas Happe}, journal={FEBS letters}, year={2010}, volume={584 3}, pages={638-42} }