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Reactions with molecular hydrogen in microorganisms: evidence for a purely organic hydrogenation catalyst

Article Abstract:

Hydrogenases catalyze the reaction of microorganisms with molecular hydrogen to yield two protons and two electrons. Carbon monoxide inhibits the activity of both Fe-only and Ni-Fe hydrogenases. Both enzymes contain at least one 4Fe-4S cluster at a site that receives electrons from H2. The rate of reactions catalyzed by the enzyme is directly proportional to the amount of cell extract added. Plasma mass spectroscopy reveals the presence of transition metals in the hydrogenase, which do not contribute towards the activity of the enzyme.

Author: Thauer, Rudolf K., Klein, Andreas R., Hartmann, Gudrun C.
Publisher: American Chemical Society
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 1996
Observations, Microorganisms, Metalloenzymes, Hydrogen

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Mechanism of molybdenum nitrogenase

Article Abstract:

The mechanism of molybdenum nitrogenase involves the Fe protein mediated transfer of electrons to the MoFe protein. This allows the reduction of the substrate by the latter. The hydrolysis of MgATPs attached to reduced Fe protein transfer one electron to the MoFe protein. The MoFe protein consists of P clusters and the FeMo cofactors clusters. The reduction of MoFe protein by one electron, decreases the metal-metal in the Fe-S clusters because the electrons do not go in the antibonding orbitals.

Author: Burgess, Barbara K., Lowe, David J.
Publisher: American Chemical Society
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 1996
Analysis, Oxidation-reduction reaction, Oxidation-reduction reactions, Nitrogenase

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