Related ArticlesNMR characterization of surface interactions in the cytochrome b5-cytochrome c complex.
Science. 1990 Feb 16;247(4944):831-3
Authors: Burch AM, Rigby SE, Funk WD, MacGillivray RT, Mauk MR, Mauk AG, Moore GR
The complex formed in solution by native and chemically modified cytochrome c with cytochrome b5 has been studied by 1H and 13C nuclear magnetic resonance spectroscopy (NMR). Contrary to predictions of recent theoretical analysis, 1H NMR spectroscopy indicates that there is no major movement of cytochrome c residue Phe82 on binding to cytochrome b5. The greater resolution provided by 13C NMR spectroscopy permits detection of small perturbations in the environments of cytochrome c residues Ile75 and Ile85 on binding with cytochrome b5, a result that is in agreement with earlier model-building experiments. As individual cytochrome c lysyl residues are resolved in the 1H NMR spectrum of N-acetimidylated cytochrome c, the interaction of this modified protein with cytochrome b5 has been studied to evaluate the number of cytochrome c lysyl residues involved in binding to cytochrome b5. The results of this experiment indicate that at least six lysyl residues are involved, two more than predicted by static model building, which indicates that cytochrome c and cytochrome b5 form two or more structurally similar 1:1 complexes in solution.
NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase [Biochemistry]
NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase
Sakamoto, K., Kamiya, M., Imai, M., Shinzawa-Itoh, K., Uchida, T., Kawano, K., Yoshikawa, S., Ishimori, K....
Date: 2011-07-26
The final interprotein electron transfer (ET) in the mammalian respiratory chain, from cytochrome c (Cyt c) to cytochrome c oxidase (CcO) is investigated by 1H-15N heteronuclear single quantum coherence spectral analysis. The chemical shift perturbation in isotope-labeled Cyt c induced by addition of unlabeled CcO indicates that the hydrophobic heme periphery and...
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[NMR paper] Characterization and calculation of a cytochrome c-cytochrome b5 complex using NMR data.
Characterization and calculation of a cytochrome c-cytochrome b5 complex using NMR data.
Related Articles Characterization and calculation of a cytochrome c-cytochrome b5 complex using NMR data.
Biochemistry. 2005 Aug 9;44(31):10654-68
Authors: Deep S, Im SC, Zuiderweg ER, Waskell L
To identify the binding site for bovine cytochrome b(5) (cyt b(5)) on horse cytochrome c (cyt c), cross-saturation transfer NMR experiments were performed with (2)H- and (15)N-enriched cyt c and unlabeled cyt b(5). In addition, chemical shift changes of the cyt c...
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[NMR paper] The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 vis
The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 visualized by NMR and docking using HADDOCK.
Related Articles The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 visualized by NMR and docking using HADDOCK.
Protein Sci. 2005 Mar;14(3):799-811
Authors: Volkov AN, Ferrari D, Worrall JA, Bonvin AM, Ubbink M
The interaction of bovine microsomal ferricytochrome b5 with yeast iso-1-ferri and ferrocytochrome c has been investigated using heteronuclear NMR techniques. Chemical-shift...
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[NMR paper] 1H NMR structural characterization of the cytochrome c modifications in a micellar en
1H NMR structural characterization of the cytochrome c modifications in a micellar environment.
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Biochemistry. 2003 Dec 30;42(51):15342-51
Authors: Chevance S, Le Rumeur E, de Certaines JD, Simonneaux G, Bondon A
The interaction of cytochrome c with micelles of sodium dodecyl sulfate was studied by proton NMR spectroscopy. The protein/micelles ratio was found to be crucial in controlling the extent of the conformational changes in...
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[NMR paper] Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fr
Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fragments derived from Paracoccus denitrificans.
Related Articles Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fragments derived from Paracoccus denitrificans.
Biochemistry. 2003 May 27;42(20):6005-12
Authors: Wienk H, Maneg O, Lücke C, Pristovsek P, Löhr F, Ludwig B, Rüterjans H
The functional interactions between the various components of the respiratory chain are relatively short-lived, thus allowing high turnover numbers...
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[NMR paper] The interactions of cyanobacterial cytochrome c6 and cytochrome f, characterized by N
The interactions of cyanobacterial cytochrome c6 and cytochrome f, characterized by NMR.
Related Articles The interactions of cyanobacterial cytochrome c6 and cytochrome f, characterized by NMR.
J Biol Chem. 2002 Dec 13;277(50):48685-9
Authors: Crowley PB, Díaz-Quintana A, Molina-Heredia FP, Nieto P, Sutter M, Haehnel W, De La Rosa MA, Ubbink M
During oxygenic photosynthesis, cytochrome c(6) shuttles electrons between the membrane-bound complexes cytochrome bf and photosystem I. Complex formation between Phormidium laminosum cytochrome f and...
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[NMR paper] Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by
Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by heteronuclear NMR spectroscopy.
Related Articles Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by heteronuclear NMR spectroscopy.
Biochemistry. 2001 Jun 19;40(24):7069-76
Authors: Worrall JA, Kolczak U, Canters GW, Ubbink M
The interaction of yeast iso-1-cytochrome c with its physiological redox partner cytochrome c peroxidase has been investigated using heteronuclear NMR techniques. Chemical shift perturbations for both...
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[NMR paper] The identification of cation-binding domains on the surface of microsomal cytochrome
The identification of cation-binding domains on the surface of microsomal cytochrome b5 using 1H-NMR paramagnetic difference spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles The identification of cation-binding domains on the surface of microsomal cytochrome b5 using 1H-NMR paramagnetic difference spectroscopy.
Eur J Biochem. 1992 Jan 15;203(1-2):211-23
Authors: Whitford D
One-dimensional and two-dimensional 1H-NMR...
NMR characterization of surface interactions in the cytochrome b5-cytochrome c comple
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