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Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/1660

Título: A further investigation of the cytochrome b5–cytochrome c complex
Autor: Moura, José J. G.
Banci, Lucia
Bertini, Ivano
Felli, Isabella C.
Krippahl, Ludwig
Kubicek, Karel
Rosato, Antonio
Palavras-chave: Cytochrome b5
Cytochrome c
Electron transfer
Protein–protein interaction
Protein recognition
Issue Date: 2003
Editora: SBIC
Resumo: The interaction of reduced rabbit cytochrome b5 with reduced yeast iso-1 cytochrome c has been studied through the analysis of 1H–15N HSQC spectra, of 15N longitudinal (R1) and transverse (R2) 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 b5 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 b5.
Descrição: J Biol Inorg Chem (2003) 8: 777–786
URI: http://hdl.handle.net/10362/1660
ISSN: 1432-1327
Appears in Collections:FCT: DQ - Artigos em revista internacional com arbitragem científica

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