Hyperfine coupling of 17O to Mo(V) in the rapid epr signal of xanthine oxidase: Evidence for an oxygen ligand of the metal |
| |
Authors: | Steven Gutteridge J.Paul G. Malthouse Robert C. Bray |
| |
Affiliation: | School of Molecular Sciences, University of SussexBrightonU.K. |
| |
Abstract: | The spectrum of the Rapid Mo(V) electron paramagnetic resonance signal from xanthine oxidase dissolved in 17O-enriched water is presented. Difference technqiues have been used to eliminate the 16O contribution. Clearly observed structure in the spectrum is attributed to moderately strong hyperfine coupling of one oxygen atom to molybdenum. Though complete interpretation of the spectrum has not been attempted, one component of A(17O) is about 1.6 mT. The possibility that the oxygen is present in a MoOH group, whose proton is the strongly-coupled proton of the Rapid signal, is discussed. |
| |
Keywords: | Address reprint requests to: Dr. R.C. Bray School of Molecular Sciences University of Sussex Falmer Brighton BN1 9QJ. U.K. |
本文献已被 ScienceDirect 等数据库收录! |