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The chemical and biological versatility of riboflavin.
- V. Massey
- Chemistry, MedicineBiochemical Society transactions
- 1 August 2000
The chemical versatility of flavoproteins is clearly controlled by specific interactions with the proteins with which they are bound, and one of the main thrusts of current research is to try to define the nature of these interactions, and to understand in chemical terms the various steps involved in catalysis by flavoprotein enzymes.
Activation of molecular oxygen by flavins and flavoproteins.
- V. Massey
- Chemistry, MedicineThe Journal of biological chemistry
- 9 September 1994
Clearly the reactivity of the reduced flavin with 0, is modulated by the protein environment in which i t is located, both in terms of rates and products of the reaction.
The microestimation of succinate and the extinction coefficient of cytochrome c.
- V. Massey
- Chemistry, MedicineBiochimica et biophysica acta
Mechanisms of flavoprotein-catalyzed reactions.
This review describes the best studied of Flavoproteins mechanisms and discusses factors possibly governing reactivity and specificity.
Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase
- J. Wang, M. Ortiz-Maldonado, B. Entsch, V. Massey, D. Ballou, D. Gatti
- Chemistry, MedicineProceedings of the National Academy of Sciences…
- 22 January 2002
It is shown that in the absence of substrate, the large βαβ domain and the smaller sheet domain separate slightly, and the flavin swings out to a more exposed position to open an aqueous channel from the solvent to the protein interior, showing how complex dynamics can play a central role in catalysis by enzymes.
On the mechanism of inactivation of xanthine oxidase by allopurinol and other pyrazolo[3,4-d]pyrimidines.
- V. Massey, H. Komai, G. Palmer, G. Elion
- Medicine, ChemistryThe Journal of biological chemistry
- 10 June 1970
It is concluded that the best preparations of xanthine oxidase so far obtained contain only 75 to 80% functional active sites, even though they possess their full complement of flavin, molybdenum, and iron-sulfur components.
PURIFICATION AND PROPERTIES OF THE GLUCOSE OXIDASE FROM ASPERGILLUS NIGER.
Mechanistic studies of cyclohexanone monooxygenase: chemical properties of intermediates involved in catalysis.
The rate-determining step in catalysis was shown to be the release of NADP from the oxidized enzyme, which is consistent with a Baeyer-Villiger rearrangement mechanism for the enzymatic oxygenation of cyclohexanone.
On the reaction mechanism of yeast glutathione reductase.
Some studies with glutathione reductase are reported which indicate that this enzyme does in fact possess a basically identical reaction mechanism to that of lipoyl dehydrogenase.