Redox and spectroscopic properties of oxidized MoFe protein from Azotobacter vinelandii
Autor: | S. Lough, G. D. Watt, A. Burns, D. L. Tennent |
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Rok vydání: | 1980 |
Předmět: |
Electrolysis
Molybdoferredoxin Azotobacter biology Chemistry Electron Spin Resonance Spectroscopy biology.organism_classification Photochemistry Biochemistry Redox Cofactor law.invention Metal Azotobacter vinelandii law visual_art biology.protein visual_art.visual_art_medium Ferredoxins Selective reduction Electron paramagnetic resonance Oxidation-Reduction |
Zdroj: | Biochemistry. 19(21) |
ISSN: | 0006-2960 |
Popis: | The MoFe protein from Azotobacter vinelandii undergoes a six-electron oxidation by various organic dye oxidants with full retention of initial activity. Reduction of the oxidized protein by S2O42- and by controlled potential electrolysis indicates the presence of two reduction regions at -290 and -480 mV, each requiring three electrons for complete reaction. Control of the oxidation conditions provides a means for preparing two distinct MoFe protein species selectively oxidized by three electrons. Selective reduction of the redox region at -290 mV causes development of the EPR signal associated with fully reduced MoFe protein while reduction at -480 mV produces a change in the visible spectrum but has no effect on the EPR signal intensity. Kinetic differences for reduction of the two redox regions indicate that the cofactor region undergoes a more rapid reaction with reductant than the other metal redox sites. |
Databáze: | OpenAIRE |
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