ArticleProtein engineering, design & selection : PEDS2012
Fusing two cytochromes b of Rhodobacter capsulatus cytochrome bc1 using various linkers defines a set of protein templates for asymmetric mutagenesis.
Article in Protein engineering, design & selection : PEDS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed.
- Catalytic Reactions and Energy Conservation in the CytochromeChemical reviews · 2021Review
- The High-Spin HemeFrontiers in chemistry · 2021Article
- A spontaneous mitonuclear epistasis converging on Rieske Fe-S protein exacerbates complex III deficiency in mice.Nature communications · 2020Article
- 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
- Mitochondrial disease-related mutations at the cytochrome b-iron-sulfur protein (ISP) interface: Molecular effects on the large-scale motion of ISP and superoxide generation studied in Rhodobacter capsulatus cytochrome bc1.Biochimica et biophysica acta · 2016Article
- Tuning of Hemes b Equilibrium Redox Potential Is Not Required for Cross-Membrane Electron Transfer.The Journal of biological chemistry · 2016Article
- Mitochondrial Disease-related Mutation G167P in Cytochrome b of Rhodobacter capsulatus Cytochrome bc1 (S151P in Human) Affects the Equilibrium Distribution of [2Fe-2S] Cluster and Generation of Superoxide.The Journal of biological chemistry · 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
- A robust genetic system for producing heterodimeric native and mutant cytochrome bc(1).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
- Enzymatic activities of isolated cytochrome bc₁-like complexes containing fused cytochrome b subunits with asymmetrically inactivated segments of electron transfer chains.Biochemistry · 2012Article
- The mechanism of ubihydroquinone oxidation at the Qo-site of the cytochrome bc1 complex.Biochimica et biophysica actaReview
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Cytochrome bc(1) (mitochondrial complex III), one of the key enzymes of biological energy conversion, is a functional homodimer in which each monomer contains three catalytic subunits: cytochrome c(1), the iron-sulfur subunit and cytochrome b. The latter is composed of eight transmembrane α-helices which, in duplicate, form a hydrophobic core of a dimer. We show that two cytochromes b can be fused into one 16-helical subunit using a number of different peptide linkers that vary in length but all connect the C-terminus of one cytochrome with the N-terminus of the other. The fusion proteins replace two cytochromes b in the dimer defining a set of available protein templates for introducing mutations that allow breaking symmetry of a dimer. A more detailed comparison of the form with the shortest, 3 amino acid, linker to the form with 12 amino acid linker established that both forms display similar level of structural plasticity to accommodate several, but not all, asymmetric patterns of mutations that knock out individual segments of cofactor chains. While the system based on a fused gene does not allow for the assessments of the functionality of electron-transfer paths in vivo, the family of proteins with fused cytochrome b offers attractive model for detailed investigations of molecular mechanism of catalysis at in vitro/reconstitution level.
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