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H2 turnover at the [FeFe]-hydrogenase cofactor (H-cluster) is assumed to follow a reversible heterolytic mechanism, first yielding a proton and a hydrido-species which again is double-oxidized to release another proton. Three of the four presumed catalytic intermediates (Hox, Hred/Hred and Hsred) were characterized, using various spectroscopic techniques.(More)
The [FeFe]-hydrogenases of bacteria and algae are the most efficient hydrogen conversion catalysts in nature. Their active-site cofactor (H-cluster) comprises a [4Fe-4S] cluster linked to a unique diiron site that binds three carbon monoxide (CO) and two cyanide (CN-) ligands. Understanding microbial hydrogen conversion requires elucidation of the interplay(More)
The six-iron cofactor of [FeFe]-hydrogenases (H-cluster) is the most efficient H2-forming catalyst in nature. It comprises a diiron active site with three carbon monoxide (CO) and two cyanide (CN(-)) ligands in the active oxidized state (Hox) and one additional CO ligand in the inhibited state (Hox-CO). The diatomic ligands are sensitive reporter groups for(More)
Growth of Escherichia coli BL21 in a glycerol minimal medium was accelerated following supplementation with trace amounts of amino acid (0.35 mM). Of 12 amino acids tested, Arg and Ser gave the highest response, increasing cell growth by 63 and 53 %, respectively, compared to control cells. The ability of amino acids to accelerate cell growth was(More)
[FeFe]-Hydrogenases contain a H2-converting cofactor (H-cluster) in which a canonical [4Fe-4S] cluster is linked to a unique diiron site with three carbon monoxide (CO) and two cyanide (CN-) ligands (e.g., in the oxidized state, Hox). There has been much debate whether reduction and hydrogen binding may result in alternative rotamer structures of the diiron(More)
[FeFe]‑hydrogenases are superior hydrogen conversion catalysts. They bind a cofactor (H-cluster) comprising a four‑iron and a diiron unit with three carbon monoxide (CO) and two cyanide (CN-) ligands. Hydrogen (H2) and oxygen (O2) binding at the H-cluster was studied in the C169A variant of [FeFe]‑hydrogenase HYDA1, in comparison to the active oxidized(More)
[FeFe]-hydrogenases catalyze the uptake and release of molecular hydrogen (H2) at a unique iron-sulfur cofactor. The absence of electrochemical overpotential in the H2 release reaction makes [FeFe]-hydrogenases a prime example of efficient biocatalysis. However, the molecular proceedings of hydrogen turnover are not understood yet. In this study, we(More)
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