The cytochrome b Zn binding amino acid residue histidine 291 is essential for ubihydroquinone oxidation at the Qo site of bacterial cytochrome bc1
| Autor: | Francesco Francia, Marco Malferrari, Fevzi Daldal, Pascal Lanciano, Stefan Steimle, Giovanni Venturoli |
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| Přispěvatelé: | Francia, Francesco, Malferrari, Marco, Lanciano, Pascal, Steimle, Stefan, Daldal, Fevzi, Venturoli, Giovanni |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Ubiquinol Cytochrome Biophysics Ubiquinol cytochrome c oxidoreductase Biochemistry 03 medical and health sciences chemistry.chemical_compound Oxidoreductase Binding site Cytochrome bc1 complex Histidine chemistry.chemical_classification 030102 biochemistry & molecular biology biology Cytochrome bc1 Zn binding Bacterial photosynthesis and respiration Qo site inactivation and proton release Cell Biology enzymes and coenzymes (carbohydrates) 030104 developmental biology Biophysic chemistry Membrane protein complex Coenzyme Q – cytochrome c reductase biology.protein |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1857:1796-1806 |
| ISSN: | 0005-2728 |
| DOI: | 10.1016/j.bbabio.2016.08.007 |
| Popis: | The ubiquinol:cytochrome (cyt) c oxidoreductase (or cyt bc1) is an important membrane protein complex in photosynthetic and respiratory energy transduction. In bacteria such as Rhodobacter capsulatus it is constituted of three subunits: the iron-sulfur protein, cyt b and cyt c1, which form two catalytic domains, the Qo (hydroquinone (QH2) oxidation) and Qi (quinone (Q) reduction) sites. At the Qo site, the pathways of bifurcated electron transfers emanating from QH2 oxidation are known, but the associated proton release routes are not well defined. In energy transducing complexes, Zn2+ binding amino acid residues often correlate with proton uptake or release pathways. Earlier, using combined EXAFS and structural studies, we identified Zn coordinating residues of mitochondrial and bacterial cyt bc1. In this work, using the genetically tractable bacterial cyt bc1, we substituted each of the proposed Zn binding residues with non-protonatable side chains. Among these mutants, only the His291Leu substitution destroyed almost completely the Qo site catalysis without perturbing significantly the redox properties of the cofactors or the assembly of the complex. In this mutant, which is unable to support photosynthetic growth, the bifurcated electron transfer reactions that result from QH2 oxidation at the Qo site, as well as the associated proton(s) release, were dramatically impaired. Based on these findings, on the putative role of His291 in liganding Zn, and on its solvent exposed and highly conserved position, we propose that His291 of cyt b is critical for proton release associated to QH2 oxidation at the Qo site of cyt bc1. |
| Databáze: | OpenAIRE |
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