Structure-function relationships of alternative nitrogenases
Article Abstract:
Vanadium nitrogenases have similar structures and redox centers as those of molybdenum nitrogenases. The interactions of gamma-subunit in the V-system are weak in the VFe protein, and give rise to active species with a single cofactor center. The Fe nitrogenase supports the growth of organisms on N2. It has low activity towards the reduction of N2 that involves the heterometal present in low concentration. Spectroscopic analysis reveals the presence of P clusters in these enzymes.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 1996
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The potential of palladacycles: More than just precatalysts
Article Abstract:
A discussion on isolated and well-defined compounds that contain a Pd-C bond stabilized by the intramolecular coordination of one or two neutral donor atoms, that is, the organic moiety acts as a C-anionic four-electron donor ligand or as a C-anionic s ix-electron donor ligand is presented. The main achievements, potential, and limitations of palladacycles are critically evaluated.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2005
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Mechanistic studies on synthetic Fe-S-based clusters and their relevance to the action of nitrogenases
Article Abstract:
The mechanistic chemistry of Fe-S-based clusters is discussed. Emphasis is laid on the reactions that are of most relevance to the role of Fe-S clusters as substrate binding and transformation sites such as substitution, protonation, binding of small molecules and ions, and transformation by coupled electron- and proton-transfer reactions.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2005
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