@article {2397,
	title = {A further investigation of the cytochrome b5-cytochrome c complex},
	journal = {J Biol Inorg Chem},
	volume = {8},
	number = {7},
	year = {2003},
	note = {<p>0949-8257 (Print)0949-8257 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}t</p>
},
	month = {Sep},
	pages = {777-86},
	abstract = {<p>The interaction of reduced rabbit cytochrome b(5) with reduced yeast iso-1 cytochrome c has been studied through the analysis of (1)H-(15)N HSQC spectra, of (15)N longitudinal ( R(1)) and transverse ( R(2)) relaxation rates, and of the solvent exchange rates of protein backbone amides. For the first time, the adduct has been investigated also from the cytochrome c side. The analysis of the NMR data was integrated with docking calculations. The result is that cytochrome b(5) has two negative patches capable of interacting with a single positive surface area of cytochrome c. At low protein concentrations and in equimolar mixture, two different 1:1 adducts are formed. At high concentration and/or with excess cytochrome c, a 2:1 adduct is formed. All the species are in fast exchange on the scale of differences in chemical shift. By comparison with literature data, it appears that the structure of one 1:1 adduct changes with the origin or primary sequence of cytochrome b(5).</p>
},
	keywords = {*Protein Interaction Mapping, Animals, Computer Simulation, Cytochromes b5/*chemistry, Cytochromes c/*chemistry, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Rabbits},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=12884088 },
	author = {Banci, L. and Bertini, I. and Felli, I. C. and Krippahl, L. and Kubicek, K. and Moura, J. J. and Rosato, A.}
}
