Role of Hydrophobic Interactions in the EncounterComplex Formation of the Plastocyanin and Cytochrome f Complex Revealed by Paramagnetic NMR Spectroscopy
Role of Hydrophobic Interactions in the EncounterComplex Formation of the Plastocyanin and Cytochrome f Complex Revealed by Paramagnetic NMR Spectroscopy
[NMR paper] Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
J Am Chem Soc. 2013 Apr 29;
Authors: Scanu S, Förster J, Ullmann GM, Ubbink M
Abstract
Protein complex formation is thought to be at least a two-step process, in which the active complex is preceded by the formation of an encounter complex....
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05-01-2013 11:46 AM
[NMR paper] Substrate-Modulated Cytochrome P450 17A1 and Cytochrome b5 Interactions Revealed by NMR.
Substrate-Modulated Cytochrome P450 17A1 and Cytochrome b5 Interactions Revealed by NMR.
Related Articles Substrate-Modulated Cytochrome P450 17A1 and Cytochrome b5 Interactions Revealed by NMR.
J Biol Chem. 2013 Apr 25;
Authors: Estrada DF, Laurence JS, Scott EE
Abstract
The membrane heme protein cytochrome b5 (b5) can enhance, inhibit, or have no effect on cytochrome P450 (P450) catalysis, depending on the specific P450, substrate, and reaction conditions, but the structural basis remains unclear. Herein the interactions between the...
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04-27-2013 01:56 PM
Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy
Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy
Abstract Cytochrome c (Cc) is a soluble electron carrier protein, transferring reducing equivalents between Cc reductase and Cc oxidase in eukaryotes. In this work, we assessed the structural differences between reduced and oxidized Cc in solution by paramagnetic NMR spectroscopy. First, we have obtained nearly-complete backbone NMR resonance assignments for iso-1-yeast Cc and horse Cc in both oxidation states. These were further used to derive pseudocontact shifts (PCSs) arising...
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02-13-2012 02:34 AM
[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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12-01-2010 06:56 PM
[NMR paper] The stability of the cytochrome c scaffold as revealed by NMR spectroscopy.
The stability of the cytochrome c scaffold as revealed by NMR spectroscopy.
Related Articles The stability of the cytochrome c scaffold as revealed by NMR spectroscopy.
J Inorg Biochem. 2004 May;98(5):814-23
Authors: Berners-Price SJ, Bertini I, Gray HB, Spyroulias GA, Turano P
NMR spectroscopy was used to study the effect of guanidinium chloride on the unfolding of horse heart and yeast iso-1 cytochrome c under mild alkaline conditions. The structural changes on the horse heart protein were detected through NOESY (Nuclear Overhauser Effect...
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11-24-2010 09:51 PM
[NMR paper] Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis
Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
Biochemistry. 1997 May 27;36(21):6326-35
Authors: Ubbink M, Bendall DS
The complexes of horse ferrous and ferric cytochrome c with Cd-substituted pea plastocyanin have been characterized by nuclear magnetic resonance, in order to determine the binding sites and to study...
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08-22-2010 03:31 PM
[NMR paper] Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis
Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
Biochemistry. 1997 May 27;36(21):6326-35
Authors: Ubbink M, Bendall DS
The complexes of horse ferrous and ferric cytochrome c with Cd-substituted pea plastocyanin have been characterized by nuclear magnetic resonance, in order to determine the binding sites and to study...
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08-22-2010 03:03 PM
[NMR paper] Ca2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by m
Ca2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by mutagenesis and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Ca2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by mutagenesis and NMR spectroscopy.
J Biol Chem. 1995 Sep 1;270(35):20643-52
Authors: Moser MJ, Lee SY, Klevit RE, Davis TN
As a first step toward identifying the important structural elements of...
Role of Hydrophobic Interactions in the EncounterComplex Formation of the Plastocyanin and Cytochrome f Complex Revealed by Paramagnetic NMR Spectroscopy
Linear Mode
