Enzymatic and Electron Transfer Activities in Crystalline Protein Complexes
| Autor: | F. Scott Mathews, Ditlev E. Brodersen, Zhi-wei Chen, Barbara Morini, R. C. E. Durley, Gian Luigi Rossi, Victor L. Davidson, Angelo Merli |
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| Rok vydání: | 1996 |
| Předmět: |
Amicyanin
Cytochrome Macromolecular Substances Cytochrome c Group Heme Photochemistry Biochemistry Protein Structure Secondary Electron Transport chemistry.chemical_compound Electron transfer Bacterial Proteins Tryptophan tryptophylquinone Methylamine dehydrogenase Indolequinones Molecular Biology Ternary complex Oxidoreductases Acting on CH-NH Group Donors Binding Sites biology Quinones Tryptophan Cell Biology Electron transport chain Models Structural chemistry Spectrophotometry biology.protein Crystallization Copper |
| Zdroj: | Journal of Biological Chemistry. 271:9177-9180 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.271.16.9177 |
| Popis: | Enzymatic and electron transfer activities have been studied by polarized absorption spectroscopy in single crystals of both binary and ternary complexes of methylamine dehydrogenase (MADH) with its redox partners. Within the crystals, MADH oxidizes methylamine, and the electrons are passed from the reduced tryptophan tryptophylquinone (TTQ) cofactor to the copper of amicyanin and to the heme of cytochrome c551i via amicyanin. The equilibrium distribution of electrons among the cofactors, and the rate of heme reduction after reaction with substrate, are both dependent on pH. The presence of copper in the ternary complex is not absolutely required for electron transfer from TTQ to heme, but its presence greatly enhances the rate of electron flow to the heme. |
| Databáze: | OpenAIRE |
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