Electron-spin-resonance evidence for interaction of protons with Mo(V) in reduced forms of xanthine oxidase
- 1 April 1968
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 107 (4) , 601-602
- https://doi.org/10.1042/bj1070601
Abstract
The form at X-band frequencies of the rapidly appearing ([image]a,/8[image] type) signal varies slightly according to the substrate employed. Some of these spectra were examined at 35 GHz [ microwave frequency] and in deuterium oxide, and the results confirm that in all cases interaction of exchangeable hydrogens with molybdenum is involved. However, it is clear that there are small deviations from the apparent axial symmetry noted by Bray & Meriwether. Further, with most substrates there must be 2 overlapping spectra contributing, though a single spectrum predominates with purine at pHIO, with gz:l-992,This publication has 4 references indexed in Scilit:
- Improved xanthine oxidase purificationBiochimica et Biophysica Acta (BBA) - Enzymology, 1967
- Electron Spin Resonance of Xanthine Oxidase Substituted with Molybdenum-95Nature, 1966
- Molybdenum–Thiol Complexes as Models for Molybdenum Bound in EnzymesNature, 1966
- DIRECT STUDIES ON ELECTRON TRANSFER SEQUENCE IN XANTHINE OXIDASE BY ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY .I. TECHNIQUES + DESCRIPTION OF SPECTRA1964