Mössbauer and EPR Study of Recombinant Acetyl-CoA Synthase from Moorella thermoacetica
| Autor: | Ivan V. Surovtsev, Audria Stubna, Paul A. Lindahl, Eckard Münck, Matthew R Bramlett, Xiangshi Tan |
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| Rok vydání: | 2006 |
| Předmět: |
education.field_of_study
biology Chemistry Inorganic chemistry Population biology.organism_classification Dithionite Biochemistry law.invention Crystallography chemistry.chemical_compound Tetramer Catalytic cycle law Moorella thermoacetica Electron paramagnetic resonance education G alpha subunit Methyl group |
| Zdroj: | Biochemistry. 45:8674-8685 |
| ISSN: | 1520-4995 0006-2960 |
| Popis: | Mossbauer and EPR spectroscopies were used to study the electronic structure of the A-cluster from recombinant acetyl-CoA synthase (the alpha subunit of the alpha2beta2 acetyl-CoA synthase/CO dehydrogenase). Once activated with Ni, these subunits have properties mimicking those associated with the alpha2beta2 tetramer, including structural heterogeneities. The Fe4S4 portion of the A-cluster in oxidized, methylated, and acetylated states was in the 2+ core oxidation state. Upon reduction with dithionite or Ti3+ citrate, samples of Ni-activated alpha developed the ability to accept a methyl group. Corresponding Mossbauer spectra exhibited two populations of A-clusters; roughly, 70% contained [Fe4S4]1+ cubanes, while approximately 30% contained [Fe4S4]2+ cubanes, suggesting an extremely low [Fe4S4](1+/2+) reduction potential for the 30% portion (perhaps |
| Databáze: | OpenAIRE |
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