Splitting molecular hydrogen

Article Abstract:

Analysis of the structure of Desulfovibrio gigas hydrogenase, which functions as a catalyst for hydrogen production and consumption, reveals a catalytic hydrogen-binding site that has two metal centers, of which one contains iron and the other is occupied by a nickel ion coordinated to four cysteine ligands of proteins. The iron atom at the other center coordinates two bridging cysteines and other non-protein ligands. Hydrogen, on reacting with the hydrogenase, is heterolytically cleaved to yield a proton and an anhydride.

Analysis, Molecular structure, Scission (Chemistry)

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The enzyme at the end of the food chain

Article Abstract:

The structure of the methyl-coenzyme M reductase has been identified by researchers. The mechanism of the organometallic reaction is shown by the nickel centre's structure and substrate interaction. The research demonstrates why and how methane is made by methanogens. The methanogens' methane-generating process involves free radicals and nickels which are uncommon in contemporary enzymes, suggesting that the new structure identifies an ancient form of metabolism.

Methanobacteriaceae, Methanogens

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Hydrogenase sophistication

Article Abstract:

Hydrogenases are central to the energy metabolism of anaerobic bacteria. The iron-only (Fe)-hydrogenases are difficult to study due to their sensitivity to oxygen. Peters and colleagues and Nicolet and colleagues have determined structures of (Fe)-hydrogenases from Clostridium pasteurianum and Desulfovibrio desulfuricans. They have defined the transfer pathway for hydrons to the H-cluster, comprising amino-acid sidechains and protein-bound water molecules.

Usage, Clostridium, Proteins, Hydrogen

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