ArticleBiochemistry2012
Enzymatic activities of isolated cytochrome bc₁-like complexes containing fused cytochrome b subunits with asymmetrically inactivated segments of electron transfer chains.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Distinct ubiquinone binding at the oxidation and reduction sites of cytochrome bcProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Decoding the Hot-Mitochondrion Paradox.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Long-range charge transfer mechanism of the IIINature communications · 2024Article
- Article
- Catalytic Reactions and Energy Conservation in the CytochromeChemical reviews · 2021Review
- The High-Spin HemeFrontiers in chemistry · 2021Article
- pH and Potential Transients of the bcThe journal of physical chemistry. B · 2017Article
- Distinct properties of semiquinone species detected at the ubiquinol oxidation Qo site of cytochrome bc1 and their mechanistic implications.Journal of the Royal Society, Interface · 2016Review
- Tuning of Hemes b Equilibrium Redox Potential Is Not Required for Cross-Membrane Electron Transfer.The Journal of biological chemistry · 2016Article
- Effect of H bond removal and changes in the position of the iron-sulphur head domain on the spin-lattice relaxation properties of the [2Fe-2S](2+) Rieske cluster in cytochrome bc(1).Physical chemistry chemical physics : PCCP · 2015Article
- 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
- Hybrid fusions show that inter-monomer electron transfer robustly supports cytochrome bc1 function in vivo.Biochemical and biophysical research communications · 2014Article
- A map of dielectric heterogeneity in a membrane protein: the hetero-oligomeric cytochrome b6f complex.The journal of physical chemistry. B · 2014Article
- Intermonomer electron transfer between the b hemes of heterodimeric cytochrome bc(1).Biochemistry · 2013Article
- A robust genetic system for producing heterodimeric native and mutant cytochrome bc(1).Biochemistry · 2013Article
- Triplet state of the semiquinone-Rieske cluster as an intermediate of electronic bifurcation catalyzed by cytochrome bc1.Biochemistry · 2013Article
- Catalytically-relevant electron transfer between two hemes bL in the hybrid cytochrome bc1-like complex containing a fusion of Rhodobacter sphaeroides and capsulatus cytochromes b.Biochimica et biophysica acta · 2013Article
- Role of the -PEWY-glutamate in catalysis at the Q(o)-site of the Cyt bc(1) complex.Biochimica et biophysica acta · 2013Article
- Inter-monomer electron transfer is too slow to compete with monomeric turnover in bc(1) complex.Biochimica et biophysica acta · 2012Article
- The mechanism of ubihydroquinone oxidation at the Qo-site of the cytochrome bc1 complex.Biochimica et biophysica actaReview
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4 authors at 1 institution in 1 country.
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Abstract
Homodimeric structure of cytochrome bc₁, a common component of biological energy conversion systems, builds in four catalytic quinone oxidation/reduction sites and four chains of cofactors (branches) that, connected by a centrally located bridge, form a symmetric H-shaped electron transfer system. The mechanism of operation of this complex system is under constant debate. Here, we report on isolation and enzymatic examination of cytochrome bc₁-like complexes containing fused cytochrome b subunits in which asymmetrically introduced mutations inactivated individual branches in various combinations. The structural asymmetry of those forms was confirmed spectroscopically. All the asymmetric forms corresponding to cytochrome bc₁ with partial or full inactivation of one monomer retain high enzymatic activity but at the same time show a decrease in the maximum turnover rate by a factor close to 2. This strongly supports the model assuming independent operation of monomers. The cross-inactivated form corresponding to cytochrome bc₁ with disabled complementary parts of each monomer retains the enzymatic activity at the level that, for the first time on isolated from membranes and purified to homogeneity preparations, demonstrates that intermonomer electron transfer through the bridge effectively sustains the enzymatic turnover. The results fully support the concept that electrons freely distribute between the four catalytic sites of a dimer and that any path connecting the catalytic sites on the opposite sides of the membrane is enzymatically competent. The possibility to examine enzymatic properties of isolated forms of asymmetric complexes constructed using the cytochrome b fusion system extends the array of tools available for investigating the engineering of dimeric cytochrome bc₁ from the mechanistic and physiological perspectives.
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