Related ArticlesInteraction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by [15N, 1H] 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 15N and 1H nuclei arising from the interaction of isotopically enriched 15N cytochrome c with cytochrome c peroxidase have been observed. For the diamagnetic, ferrous cytochrome c, 34 amides are affected by binding, corresponding to residues at the front face of the protein and in agreement with the interface observed in the 1:1 crystal structure of the complex. In contrast, for the paramagnetic, ferric protein, 56 amides are affected, corresponding to residues both at the front and toward the rear of the protein. In addition, the chemical shift perturbations were larger for the ferric protein. Using experimentally observed pseudocontact shifts the magnetic susceptibility tensor of yeast iso-1-cytochrome c in both the free and bound forms has been calculated with HN nuclei as inputs. In contrast to an earlier study, the results indicate that there is no change in the geometry of the magnetic axes for cytochrome c upon binding to cytochrome c peroxidase. This leads us to conclude that the additional effects observed for the ferric protein arise either from a difference in binding mode or from the more flexible overall structure causing a transmittance effect upon binding.
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] 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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11-24-2010 09:01 PM
[NMR paper] pH-dependent equilibria of yeast Met80Ala-iso-1-cytochrome c probed by NMR spectrosco
pH-dependent equilibria of yeast Met80Ala-iso-1-cytochrome c probed by NMR spectroscopy: a comparison with the wild-type protein.
Related Articles pH-dependent equilibria of yeast Met80Ala-iso-1-cytochrome c probed by NMR spectroscopy: a comparison with the wild-type protein.
Chem Biol. 1995 Jun;2(6):377-83
Authors: Banci L, Bertini I, Bren KL, Gray HB, Turano P
BACKGROUND: Cytochrome c has five distinct pH-dependent conformational states, including two alkaline forms of unknown structure. It is believed that in both of the alkaline forms a...
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[NMR paper] Studies of protein-protein association between yeast cytochrome c peroxidase and yeas
Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy.
Related Articles Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy.
Biochemistry. 1994 Oct 11;33(40):12032-41
Authors: Yi Q, Erman JE, Satterlee JD
Hydrogen-deuterium (H-D) exchange labeling and proton NMR have been applied to study the...
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[NMR paper] NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c i
NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted.
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 NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted.
Eur J Biochem. 1991 Dec 5;202(2):339-47
Authors: Thurgood AG, Davies AM, Greenwood C, Mauk AG, Smith M,...
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08-21-2010 11:12 PM
[NMR paper] NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c i
NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted.
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 NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted.
Eur J Biochem. 1991 Dec 5;202(2):339-47
Authors: Thurgood AG, Davies AM, Greenwood C, Mauk AG, Smith M,...
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[NMR paper] Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the
Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235----Asn-235 mutant.
Related Articles Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235----Asn-235 mutant.
Biochemistry. 1990 Sep 18;29(37):8797-804
Authors: Satterlee JD, Erman JE, Mauro JM, Kraut J
Proton NMR spectra of cytochrome c peroxidase (CcP) isolated from yeast (wild type) and two Escherichia coli...
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[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 yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by
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