| BANCI, Lucia, Ivano BERTINI, Isabella C FELLI, Ludwig KRIPPAHL, Karel KUBÍČEK, Jose J MOURA a Antonio ROSATO. A further investigation of the cytochrome b5-cytochrome c complex. Journal of Biological Inorganic Chemistry. Heidelberg: Springer Verlag, 2003, roč. 8, č. 7, s. 777-786. ISSN 0949-8257. |
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@article{724879,
author = {Banci, Lucia and Bertini, Ivano and Felli, Isabella C and Krippahl, Ludwig and Kubíček, Karel and Moura, Jose J and Rosato, Antonio},
article_location = {Heidelberg},
article_number = {7},
keywords = {cytochrome b5; cytochrome c; electron transfer; protein-protein interaction; protein recognition},
language = {eng},
issn = {0949-8257},
journal = {Journal of Biological Inorganic Chemistry},
title = {A further investigation of the cytochrome b5-cytochrome c complex},
url = {http://www.springerlink.com/content/lfpnxh9pw0v1l10t/},
volume = {8},
year = {2003}
}
TY - JOUR
ID - 724879
AU - Banci, Lucia - Bertini, Ivano - Felli, Isabella C - Krippahl, Ludwig - Kubíček, Karel - Moura, Jose J - Rosato, Antonio
PY - 2003
TI - A further investigation of the cytochrome b5-cytochrome c complex
JF - Journal of Biological Inorganic Chemistry
VL - 8
IS - 7
SP - 777-786
EP - 777-786
PB - Springer Verlag
SN - 09498257
KW - cytochrome b5
KW - cytochrome c
KW - electron transfer
KW - protein-protein interaction
KW - protein recognition
UR - http://www.springerlink.com/content/lfpnxh9pw0v1l10t/
L2 - http://www.springerlink.com/content/lfpnxh9pw0v1l10t/
N2 - 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.
ER -
BANCI, Lucia, Ivano BERTINI, Isabella C FELLI, Ludwig KRIPPAHL, Karel KUBÍČEK, Jose J MOURA a Antonio ROSATO. A further investigation of the cytochrome b5-cytochrome c complex. \textit{Journal of Biological Inorganic Chemistry}. Heidelberg: Springer Verlag, 2003, roč.~8, č.~7, s.~777-786. ISSN~0949-8257.
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