CYC1/YJR048W Literature Guide Help

Other names published for CYC1: iso-1-cytochrome c, YJR048W

CYC1 - Protein-protein Interactions (45)

ReferenceOther Genes Addressed
Kokhan O, et al.  (2010) The binding interface of cytochrome c and cytochrome c in the bc complex: rationalizing the role of key residues. Biophys J 99(8):2647-56
Volkov AN, et al.  (2009) Binding hot spot in the weak protein complex of physiological redox partners yeast cytochrome C and cytochrome C peroxidase. J Mol Biol 385(3):1003-13
Claypool SM, et al.  (2008) Cardiolipin defines the interactome of the major ADP/ATP carrier protein of the mitochondrial inner membrane. J Cell Biol 182(5):937-50
Solmaz SR and Hunte C  (2008) Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer. J Biol Chem 283(25):17542-9
Dabir DV, et al.  (2007) A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1. EMBO J 26(23):4801-11
Kang SA, et al.  (2006) Solvent isotope effects on interfacial protein electron transfer in crystals and electrode films. J Am Chem Soc 128(7):2346-55
Nakani S, et al.  (2006) Characterization of a covalently linked yeast cytochrome c-cytochrome c peroxidase complex: evidence for a single, catalytically active cytochrome c binding site on cytochrome c peroxidase. Biochemistry 45(32):9887-93
Nakani S, et al.  (2006) Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules. Biochemistry 45(48):14371-8
Volkov AN, et al.  (2006) From the Cover: Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR. Proc Natl Acad Sci U S A 103(50):18945-50
Volkov AN, et al.  (2005) The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 visualized by NMR and docking using HADDOCK. Protein Sci 14(3):799-811
Guo M, et al.  (2004) Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link. Proc Natl Acad Sci U S A 101(16):5940-5
Engstrom G, et al.  (2003) Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex. Biochemistry 42(10):2816-24
Sinibaldi F, et al.  (2003) Rupture of the hydrogen bond linking two Omega-loops induces the molten globule state at neutral pH in cytochrome c. Biochemistry 42(24):7604-10
Blouin C, et al.  (2002) Probing electrostatic interactions in cytochrome c using site-directed chemical modification. Biochem Cell Biol 80(2):197-203
Hunte C, et al.  (2002) Electron transfer between yeast cytochrome bc(1) complex and cytochrome c: a structural analysis. Biochim Biophys Acta 1555(1-3):21-8
Mei H, et al.  (2002) Role of the low-affinity binding site in electron transfer from cytochrome C to cytochrome C peroxidase. Biochemistry 41(12):3968-76
Morar AS, et al.  (2001) Effects of crowding by mono-, di-, and tetrasaccharides on cytochrome c-cytochrome c peroxidase binding: comparing experiment to theory. Biochemistry 40(1):281-5
Pielak GJ and Wang X  (2001) Interactions between yeast iso-1-cytochrome c and its peroxidase. Biochemistry 40(2):422-8
Worrall JA, et al.  (2001) Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by [15N, 1H] heteronuclear NMR spectroscopy. Biochemistry 40(24):7069-76
Dopner S, et al.  (1999) The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase. Eur J Biochem 261(2):379-91
Rizzo P, et al.  (1999) Antibody immunodiversity: a study on the marked specificity difference between two anti-yeast iso-1 cytochrome c monoclonal antibodies whose epitopes are closely related. J Protein Chem 18(5):523-32
Wang X and Pielak GJ  (1999) Equilibrium thermodynamics of a physiologically-relevant heme-protein complex. Biochemistry 38(51):16876-81
Moore GR, et al.  (1998) N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation. Biochem J 332 ( Pt 2)():439-49
Pearce DA and Sherman F  (1998) Degradation of yeast cytochromes c dependent and independent on its physiological partners. Arch Biochem Biophys 352(1):85-96
Sukits SF, et al.  (1997) Proton NMR assignments and magnetic axes orientations for wild-type yeast iso-1-ferricytochrome c free in solution and bound to cytochrome c peroxidase. Biochemistry 36(17):5251-9
Matthis AL and Erman JE  (1995) Cytochrome c peroxidase-catalyzed oxidation of yeast iso-1 ferrocytochrome c by hydrogen peroxide. Ionic strength dependence of the steady-state parameters. Biochemistry 34(31):9985-90
Matthis AL, et al.  (1995) Oxidation of yeast iso-1 ferrocytochrome c by yeast cytochrome c peroxidase compounds I and II. Dependence upon ionic strength. Biochemistry 34(31):9991-9
Guillemette JG, et al.  (1994) Analysis of the bimolecular reduction of ferricytochrome c by ferrocytochrome b5 through mutagenesis and molecular modelling. Biochimie 76(7):592-604
Corin AF, et al.  (1993) Effects of surface amino acid replacements in cytochrome c peroxidase on intracomplex electron transfer from cytochrome c. Biochemistry 32(11):2756-62
Hildebrandt P, et al.  (1993) Resonance Raman study of the interactions between cytochrome c variants and cytochrome c oxidase. Biochemistry 32(40):10912-22