Hybrid fusions show that inter-monomer electron transfer robustly supports cytochrome bc1 function in vivo |
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Authors: | Robert Ekiert Monika CzaplaMarcin Sarewicz Artur Osyczka |
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Affiliation: | Department of Molecular Biophysics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30-387 Kraków, Poland |
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Abstract: | Electronic connection between Qo and Qi quinone catalytic sites of dimeric cytochrome bc1 is a central feature of the energy-conserving Q cycle. While both the intra- and inter-monomer electron transfers were shown to connect the sites in the enzyme, mechanistic and physiological significance of the latter remains unclear. Here, using a series of mutated hybrid cytochrome bc1-like complexes, we show that inter-monomer electron transfer robustly sustains the function of the enzyme in vivo, even when the two subunits in a dimer come from different species. This indicates that minimal requirement for bioenergetic efficiency is to provide a chain of cofactors for uncompromised electron flux between the catalytic sites, while the details of protein scaffold are secondary. |
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Keywords: | Cytochrome bc1 Mitochondrial complex III Hybrid fusion protein Electron transfer Energy conversion |
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