Energy-converting respiratory Complex I: On the way to the molecular mechanism of the proton pump
| Autor: | Dmitry A. Bloch, Marina Verkhovskaya |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Iron-Sulfur Proteins
Models Molecular Ubiquinone Biology Biochemistry Redox Electron Transport 03 medical and health sciences Oxidoreductase Animals Humans Protein Structure Quaternary Electrochemical gradient 030304 developmental biology Exergonic reaction chemistry.chemical_classification 0303 health sciences Binding Sites Electron Transport Complex I Bacteria 030302 biochemistry & molecular biology Cell Biology Hydrogen-Ion Concentration Respiratory enzyme Transmembrane protein Enzyme structure Mitochondria 3. Good health chemistry Oxidation-Reduction Flux (metabolism) Protein Binding |
| Zdroj: | The International Journal of Biochemistry & Cell Biology. 45:491-511 |
| ISSN: | 1357-2725 |
| DOI: | 10.1016/j.biocel.2012.08.024 |
| Popis: | In respiring organisms the major energy transduction flux employs the transmembrane electrochemical proton gradient as a physical link between exergonic redox reactions and endergonic ADP phosphorylation. Establishing the gradient involves electrogenic, transmembrane H+ translocation by the membrane-embedded respiratory complexes. Among others, Complex I (NADH:ubiquinone oxidoreductase) is the most structurally complex and functionally enigmatic respiratory enzyme; its molecular mechanism is as yet unknown. Here we highlight recent progress and discuss the catalytic events during Complex I turnover in relation to their role in energy conversion and to the enzyme structure. |
| Databáze: | OpenAIRE |
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