ArticleBiophysical journal2010
The binding interface of cytochrome c and cytochrome c₁ in the bc₁ complex: rationalizing the role of key residues.
Article in Biophysical journal, 2010. 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.
- The flexible chain: regulation of structure and activity of ETC complexes defines rate of ATP synthesis and sites of superoxide generation.Biophysical reviews · 2025Review
- Diverse functions of cytochrome c in cell death and disease.Cell death and differentiation · 2024Review
- Phosphorylations and Acetylations of CytochromeCells · 2024Review
- Sometimes less is more: inhibitory infrared light during early reperfusion calms hyperactive mitochondria and suppresses reperfusion injury.Biochemical Society transactions · 2022Review
- Decoding the role of cytochrome c in metabolism of human spermatozoa by Raman imaging.Frontiers in cell and developmental biology · 2022Article
- Structural and functional insights into lysine acetylation of cytochrome c using mimetic point mutants.FEBS open bio · 2021Article
- Modulating the pro-apoptotic activity of cytochrome c at a biomimetic electrified interface.Science advances · 2021Article
- Catalytic Reactions and Energy Conservation in the CytochromeChemical reviews · 2021Review
- Post-Translational Modifications of CytochromeInternational journal of molecular sciences · 2020Review
- Cytochrome c Reductase is a Key Enzyme Involved in the Extracellular Electron Transfer Pathway towards Transition Metal Complexes in Pseudomonas Putida.ChemSusChem · 2020Article
- Article
- Cytochrome c phosphorylation: Control of mitochondrial electron transport chain flux and apoptosis.The international journal of biochemistry & cell biology · 2020Article
- Long distance electron transfer through the aqueous solution between redox partner proteins.Nature communications · 2018Article
- In vitro rejuvenation of brain mitochondria by the inhibition of actin polymerization.Scientific reports · 2018Article
- Binding Site Recognition and Docking Dynamics of a Single Electron Transport Protein: Cytochrome c2.Journal of the American Chemical Society · 2016Article
- Colin A. Wraight, 1945-2014.Photosynthesis research · 2016Article
- Modeling of interaction between cytochrome c and the WD domains of Apaf-1: bifurcated salt bridges underlying apoptosome assembly.Biology direct · 2015Article
- Molecular organization of cytochrome c2 near the binding domain of cytochrome bc1 studied by electron spin-lattice relaxation enhancement.The journal of physical chemistry. B · 2014Article
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chemical reviews · 2014Review
- Discovering co-occurring patterns and their biological significance in protein families.BMC bioinformatics · 2014Article
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Authors and funding
3 authors.
Funding
Abstract
The interaction of cytochrome c with ubiquinol-cytochrome c oxidoreductase (bc₁ complex) has been studied for >30 years, yet many aspects remain unclear or controversial. We report the first molecular dynamic simulations of the cyt c-bc₁ complex interaction. Contrary to the results of crystallographic studies, our results show that there are multiple dynamic hydrogen bonds and salt bridges in the cyt c-c₁ interface. These include most of the basic cyt c residues previously implicated in chemical modification studies. We suggest that the static nature of x-ray structures can obscure the quantitative significance of electrostatic interactions between highly mobile residues. This provides a clear resolution of the discrepancy between the structural data and functional studies. It also suggests a general need to consider dynamic interactions of charged residues in protein-protein interfaces. In addition, a novel structural change in cyt c is reported, involving residues 21-25, which may be responsible for cyt c destabilization upon binding. We also propose a mechanism of interaction between cyt c₁ monomers responsible for limiting the binding of cyt c to only one molecule per bc₁ dimer by altering the affinity of the cytochrome c binding site on the second cyt c₁ monomer.
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