ArticleBiochemical and biophysical research communications2014
Hybrid fusions show that inter-monomer electron transfer robustly supports cytochrome bc1 function in vivo.
Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Complex Interplay of Metabolic Substrates, Points of Entry into the Mitochondrial Electron Chain, and ROS Generation: A critical analysis of "Active control of mitochondrial network morphology by metabolism-driven redox state" by Singh et al. and studies replacing ETC components with yeast counterparts.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Cryo-EM structure of the four-subunitProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Catalytic Reactions and Energy Conservation in the CytochromeChemical reviews · 2021Review
- Analysis of a Functional Dimer Model of Ubiquinol Cytochrome c Oxidoreductase.Biophysical journal · 2017Article
- Identifying involvement of Lys251/Asp252 pair in electron transfer and associated proton transfer at the quinone reduction site of Rhodobacter capsulatus cytochrome bc1.Biochimica et biophysica acta · 2016Article
- Cardiolipin deficiency causes a dissociation of the b 6 c:caa 3 megacomplex in B. subtilis membranes.Journal of bioenergetics and biomembranes · 2016Article
- Tuning of Hemes b Equilibrium Redox Potential Is Not Required for Cross-Membrane Electron Transfer.The Journal of biological chemistry · 2016Article
- Electronic connection between the quinone and cytochrome C redox pools and its role in regulation of mitochondrial electron transport and redox signaling.Physiological reviews · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
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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