The allosteric protein interactions in the proton-motive function of mammalian redox enzymes of the respiratory chain
| Autor: | Sergio Papa, Francesco Papa, Giuseppe Capitanio |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Conformational change Stereochemistry Protein subunit Allosteric regulation Respiratory chain Cytochromes c1 Biochemistry Electron Transport Complex IV 03 medical and health sciences chemistry.chemical_compound Allosteric Regulation Oxidoreductase Animals Humans Heme Ubiquinone binding chemistry.chemical_classification Electron Transport Complex I 030102 biochemistry & molecular biology Proton-Motive Force General Medicine Cytochromes b 030104 developmental biology Heme A chemistry |
| Zdroj: | Biochimie. 189 |
| ISSN: | 1638-6183 |
| Popis: | Insight into mammalian respiratory complexes defines the role of allosteric protein interactions in their proton-motive activity. In cytochrome c oxidase (CxIV) conformational change of subunit I, caused by O2 binding to heme a32+-CuB+ and reduction, and stereochemical transitions coupled to oxidation/reduction of heme a and CuA, combined with electrostatic effects, determine the proton pumping activity. In ubiquinone-cytochrome c oxidoreductase (CxIII) conformational movement of Fe-S protein between cytochromes b and c1 is the key element of the proton-motive activity. In NADH-ubiquinone oxidoreductase (CxI) ubiquinone binding and reduction result in conformational changes of subunits in the quinone reaction structure which initiate proton pumping. |
| Databáze: | OpenAIRE |
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