Electron paramagnetic resonance and potentiometric studies of arsenite interaction with the molbydenum centers of xanthine oxidase, xanthine dehydrogenase, and aldehyde oxidase: a specific stabilization of the molybdenum(V) oxidation state
- 1 February 1983
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 22 (3) , 618-624
- https://doi.org/10.1021/bi00272a014
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- Electron paramagnetic resonance properties and oxidation-reduction potentials of the molybdenum, flavin, and iron-sulfur centers of chicken liver xanthine dehydrogenaseArchives of Biochemistry and Biophysics, 1980
- Comparison of the molybdenum centres of native and desulpho xanthine oxidase. The nature of the cyanide-labile sulphur atom and the nature of the proton-accepting groupBiochemical Journal, 1978
- Electron paramagnetic resonance in biochemistry. Computer simulation of spectra from frozen aqueous samplesBiochemical Journal, 1978
- Magnetic coupling of the molybdenum and iron-sulphur centres in xanthine oxidase and xanthine dehydrogenasesBiochemical Journal, 1978
- Changes in apparent pH on freezing aqueous buffer solutions and their relevance to biochemical electron-paramagnetic-resonance spectroscopyBiochemical Journal, 1977
- A new non-functional form of milk xanthine oxidase containing stable quinquivalent molybdenumBiochemical Journal, 1976
- 6 Molybdenum Iron-Sulfur Flauin Hydroxylases and Related EnzymesPublished by Elsevier ,1975
- HEPATIC ALDEHYDE OXIDASE .3. SUBSTRATE-BINDING SITE1964
- HEPATIC ALDEHYDE OXIDASE .1. PURIFICATION AND PROPERTIES1962
- Effect of arsenite and cadmium ions on xanthine oxidaseArchives of Biochemistry and Biophysics, 1961