Related ArticlesThe 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 of this small anion in the active cavity of the enzyme, possibly in the proximity of the distal histidine and the distal arginine.
[NMR paper] Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fr
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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] Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by
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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] 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.
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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] A 35Cl and 37Cl NMR study of chloride binding to the erythrocyte anion transport prot
A 35Cl and 37Cl NMR study of chloride binding to the erythrocyte anion transport protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A 35Cl and 37Cl NMR study of chloride binding to the erythrocyte anion transport protein.
Biophys Chem. 1991 Jul;40(3):329-37
Authors: Price WS, Kuchel PW, Cornell BA
Band 3, the erythrocyte anion transport protein, mediates the one-for-one exchange of bicarbonate and chloride ions across the membrane and consequently plays an...
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[NMR paper] NMR study of the active site of resting state and cyanide-inhibited lignin peroxidase
NMR study of the active site of resting state and cyanide-inhibited lignin peroxidase from Phanerochaete chrysosporium. Comparison with horseradish peroxidase.
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J Biol Chem. 1991 Aug 15;266(23):15001-8
Authors: de Ropp JS, La Mar GN, Wariishi H, Gold MH
One- and two-dimensional 1H NMR spectroscopy has been used to probe the active site of the high spin ferric resting...
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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.
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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] An NMR study of anion binding to yeast phosphoglycerate kinase.
An NMR study of anion binding to yeast phosphoglycerate kinase.
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Eur J Biochem. 1990 May 31;190(1):161-9
Authors: Fairbrother WJ, Graham HC, Williams RJ
Anion binding to yeast phosphoglycerate kinase has been investigated using 1H-NMR spectroscopy. The use of anionic paramagnetic probes. 3- and 3-, has enabled the...
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[NMR paper] Two-dimensional 1H-NMR studies of horseradish peroxidase C and its interaction with i
Two-dimensional 1H-NMR studies of horseradish peroxidase C and its interaction with indole-3-propionic acid.
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Eur J Biochem. 1990 Apr 30;189(2):351-62
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The interaction of the nitrate anion with cytochrome c peroxidase: a 15N-NMR study.
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