Evidence for the inorganic nature of the cyanolyzable sulfur of molybdenum hydroxylases.

  title={Evidence for the inorganic nature of the cyanolyzable sulfur of molybdenum hydroxylases.},
  author={Rosemarie Wahl and Krishnan Rajagopalan},
  journal={The Journal of biological chemistry},
  volume={257 3},

Properties of rabbit liver aldehyde oxidase and the relationship of the enzyme to xanthine oxidase and dehydrogenase.

It is concluded that the molybdenum centres of xanthine oxidase and aldehyde oxidase are indeed similar to one another and that such differences as exist between their molyBdenum(V) EPR signals and re-sulfuration properties are related to differences only in the substrate-binding sites.

Inhibitors of the molybdenum cofactor containing 4-hydroxybenzoyl-CoA reductase.

The results obtained revealed further insights into the active site of an unusual member of the XO family of molybdenum cofactor containing enzymes and revealed a hyperfine splitting due to magnetic coupling with two solvent-exchangeable protons in the dithionite-inhibited states.

Cyanide inactivation of hydrogenase from Azotobacter vinelandii

The results indicate that cyanide can cause a time-dependent, irreversible inactivation of hydrogenase in the oxidized, activatable state but has no effect when hydrogenase is in the reduced, active state.

Molecular characterization of human xanthine oxidoreductase: the enzyme is grossly deficient in molybdenum and substantially deficient in iron-sulphur centres.

Findings add further support to the idea that XOR protein plays a physiological role in milk equal in importance to its catalytic function as an enzyme, as well as demonstrating the importance of enzymic activity and Mo content.

Kinetic and Structural Studies of Aldehyde Oxidoreductase from Desulfovibrio gigas Reveal a Dithiolene-Based Chemistry for Enzyme Activation and Inhibition by H2O2

A combined kinetic and X-ray crystallographic study is reported to unveil the enzyme modification responsible for the inactivation and the chemistry that occurs at the Mo site when DgAOR is activated.

Cell biology of molybdenum.

4‐Hydroxybenzoyl‐Coenzyme A Reductase

The structural, electrochemical, spectroscopic, and kinetic properties of HBCR from Thauera aromatica are highlighted and compared with other members of the xanthine oxidase family in catalyzing the irreversible reduction of the substrate.