[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. The interactions in the encounter complex are usually dominated by electrostatic forces, whereas the active complex is also stabilized by non-covalent short range forces. Here, the complex of cytochrome f and plastocyanin, electron transfer proteins involved in photosynthesis, was studied using paramagnetic relaxation NMR spectroscopy. Spin labels were attached to cytochrome f and the relaxation enhancements of plastocyanin nuclei were measured, demonstrating that a large part of the cytochrome f surface area is sampled by plastocyanin. In contrast, plastocyanin is always oriented with its hydrophobic patch toward cytochrome f. The complex was visualized using ensemble docking, showing that the encounter complex is stabilized by hydrophobic as well as electrostatic interactions. The results suggest a model of electrostatic pre-orientation before the proteins make contact, followed by the formation of an encounter complex that rapidly leads to electron transfer active conformations by gradual increase of the overlap of non-polar surface areas on cytochrome f and plastocyanin. In this model the distinction between the encounter and active complexes vanishes, at least in the case of electron transfer complexes, which do not require a high degree of specificity.
PMID: 23627316 [PubMed - as supplied by publisher]
[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...
nmrlearner
Journal club
0
04-27-2013 01:56 PM
[NMR paper] Analysis of SNARE complex/Synaptotagmin-1 Interactions by One-dimensional NMR Spectroscopy.
Analysis of SNARE complex/Synaptotagmin-1 Interactions by One-dimensional NMR Spectroscopy.
Related Articles Analysis of SNARE complex/Synaptotagmin-1 Interactions by One-dimensional NMR Spectroscopy.
Biochemistry. 2013 Apr 25;
Authors: Zhou A, Brewer KD, Rizo J
Abstract
Neurotransmitter release depends critically on the Ca2+ sensor synaptotagmin-1 and the SNARE proteins syntaxin-1, synaptobrevin and SNAP-25, which mediate membrane fusion by forming tight SNARE complexes that bridge the synaptic vesicle and plasma membranes. Interactions...
nmrlearner
Journal club
0
04-27-2013 01:56 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
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy
Abstract Many biomolecular interactions proceed via a short-lived encounter state, consisting of multiple, lowly-populated species invisible to most experimental techniques. Recent development of paramagnetic relaxation enhancement (PRE) nuclear magnetic resonance (NMR) spectroscopy has allowed to directly visualize such transient intermediates in a number of protein-protein and protein-DNA complexes. Here we present an analysis of the recently published PRE NMR data for a protein complex of yeast...
nmrlearner
Journal club
0
11-06-2010 01:24 PM
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy.
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy.
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy.
J Biomol NMR. 2010 Nov 4;
Authors: Volkov AN, Ubbink M, van Nuland NA
Many biomolecular interactions proceed via a short-lived encounter state, consisting of multiple, lowly-populated species invisible to most experimental techniques. Recent development of paramagnetic relaxation enhancement (PRE) nuclear magnetic resonance (NMR) spectroscopy has allowed to directly visualize such...
nmrlearner
Journal club
0
11-05-2010 10:01 AM
[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...
nmrlearner
Journal club
0
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...