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. 1982 Apr 1;203(1):263–267. doi: 10.1042/bj2030263

Studies by electron-paramagnetic-resonance spectroscopy of the molybdenum centre of aldehyde oxidase.

R C Bray, G N George, S Gutteridge, L Norlander, J G Stell, C Stubley
PMCID: PMC1158218  PMID: 6285895

Abstract

Molybdenum(V) e.p.r. spectra from reduced forms of aldehyde oxidase were obtained and compared with those from xanthine oxidase. Inhibited and Desulpho Inhibited signals from aldehyde oxidase were fully characterized, and parameters were obtained with the help of computer simulations. These differ slightly but significantly from the corresponding parameters for the xanthine oxidase signals. Rapid type 1 and type 2 and Slow signals were obtained from aldehyde oxidase, but were not fully characterized. From the general similarities of the signals from the two enzymes, it is concluded that the ligands of molybdenum must be identical and that the overall co-ordination geometries must be closely similar in the enzymes. The striking differences in substrate specificity must relate primarily to structural differences in a part of the active centre concerned with substrate binding and not involving the catalytically important molybdenum site.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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