Document details

A further investigation of the cytochrome b5–cytochrome c complex

Author(s): Banci, Lucia cv logo 1 ; Bertini, Ivano cv logo 2 ; Moura, José J. G. cv logo 3 ; Felli, Isabella C. cv logo 4 ; Krippahl, Ludwig cv logo 5 ; Kubicek, Karel cv logo 6

Date: 2003

Persistent ID: http://hdl.handle.net/10362/8719

Origin: Repositório Institucional da UNL


Description
J Biol Inorg Chem (2003) 8: 777–786 DOI 10.1007/s00775-003-0479-y 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).
Document Type Article
Language English
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