Related ArticlesInteraction 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 but at the same time complicating the structural analysis of the complexes. Chemical shift mapping by NMR spectroscopy is a useful tool to investigate such transient contacts, since it can monitor changes in the electron-shielding properties of a protein as the result of temporary contacts with a reaction partner. In this study, we investigated the molecular interaction between two components of the electron-transfer chain from Paracoccus denitrificans: the engineered, water-soluble fragment of cytochrome c(552) and the Cu(A) domain from the cytochrome c oxidase. Comparison of [(15)N,(1)H]-TROSY spectra of the [(15)N]-labeled cytochrome c(552) fragment in the absence and in the presence of the Cu(A) fragment showed chemical shift changes for the backbone amide groups of several, mostly uncharged residues located around the exposed heme edge in cytochrome c(552). The detected contact areas on the cytochrome c(552) surface were comparable under both fully reduced and fully oxidized conditions, suggesting that the respective chemical shift changes represent biologically relevant protein-protein interactions.
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...
nmrlearner
Journal club
0
07-26-2011 11:22 PM
[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...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[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...
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[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...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[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...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[NMR paper] Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. E
Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements.
Related Articles Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements.
Biochemistry. 1991 Apr 23;30(16):3871-9
Authors: Spooner PJ, Watts A
Deuterium NMR has been used to investigate the structure and dynamic state of cytochrome c complexed with bilayers of cardiolipin. Reductive methylation was employed to prepare lysyl cytochrome c, and deuterium...
nmrlearner
Journal club
0
08-21-2010 11:16 PM
[NMR paper] NMR characterization of surface interactions in the cytochrome b5-cytochrome c comple
NMR characterization of surface interactions in the cytochrome b5-cytochrome c complex.
Related Articles NMR 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...
nmrlearner
Journal club
0
08-21-2010 10:48 PM
[NMR paper] The interaction of the nitrate anion with cytochrome c peroxidase: a 15N-NMR study.
The interaction of the nitrate anion with cytochrome c peroxidase: a 15N-NMR study.
Related Articles The interaction of the nitrate anion with cytochrome c peroxidase: a 15N-NMR study.
Spectrochim Acta A Mol Biomol Spectrosc. 1999 Feb;55A(2):415-20
Authors: Banci L, Pierattelli R
The interaction of the nitrate anion with cytochrome c peroxidase has been demonstrated by using 15N-NMR spectroscopy. The results indicate that the nitrate anion binds to the protein in a specific binding site and are consistent with the hypothesis of an interaction...
Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fr
Linear Mode
