Model Studies

  • C. A. Mcauliffe
Part of the Aspects of Inorganic Chemistry book series


Knowledge of the ligand environment of molybdenum in its enzymes is, to say the least, scanty. Such evidence as there is, based on comparisons between the e.p.r. parameters of, for example, xanthine oxidase and molybdenum complexes of sulphur ligands (see table 23, page 216), is thought to indicate molybdenum-sulphur binding. Most attention has been concentrated on cysteine as the obvious candidate for the role of a sulphur-containing biological ligand. Interest has also been shown in the potential alternative binding site for molybdenum, namely a flavin moiety, on the grounds that several of the molybdenum enzymes are metaloflavoproteins.


Xanthine Oxidase Molecular Nitrogen Nitrogen Molecule Binuclear Complex Molybdenum Atom 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Palgrave Macmillan, a division of Macmillan Publishers Limited 1975

Authors and Affiliations

  • C. A. Mcauliffe
    • 1
  1. 1.Institute of Science and TechnologyUniversity of ManchesterUK

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