A further investigation of the cytochrome b5-cytochrome c
complex

J 2003

A further investigation of the cytochrome b5-cytochrome c complex

BANCI, Lucia, Ivano BERTINI, Isabella C FELLI, Ludwig KRIPPAHL, Karel KUBÍČEK et. al.

Základní údaje

Originální název

A further investigation of the cytochrome b5-cytochrome c complex

Název česky

Další studium komplexu tvořeným cytochromem b5 s cytochromem c

Autoři

BANCI, Lucia (380 Itálie), Ivano BERTINI (380 Itálie), Isabella C FELLI (380 Itálie), Ludwig KRIPPAHL (276 Německo), Karel KUBÍČEK (203 Česká republika, garant), Jose J MOURA (620 Portugalsko) a Antonio ROSATO (380 Itálie)

Vydání

Journal of Biological Inorganic Chemistry, Heidelberg, Springer Verlag, 2003, 0949-8257

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10610 Biophysics

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.905

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

cytochrome b5; cytochrome c; electron transfer; protein-protein interaction; protein recognition

Štítky

cytochrome b5, cytochrome c, electron transfer, protein recognition, protein-protein interaction

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 12. 9. 2007 15:50, doc. Mgr. Karel Kubíček, PhD.

Anotace

ORIG CZ

V originále

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.

Česky

Interakce mezi cytochromem b5 s redukovaným cytochromem c byla studována analýzou 1H-15N HSQC NMR spekter, 15N longitudinálních (R1) a transversálních (R2) relaxačních rychlostí a analýzou rychlostí výmeny amidických protonů proteinové páteře se solventem. V této práci byl poprvé studován výsledný komplex ze strany cytochromu c. NMR analýza byla doplněna dockingem. Při nízkých koncentracích proteinů a ekvimolární směsi se tvoří dva různé komplexy 1:1. Při vysokých koncentracích a/nebo při nadbytku cytochromu c je tvořen komplex 2:1. Všechnz vzniklé komplexy jsou v režimu rychlé výměny na NMR škále. Při porovnání s daty uvedenými v literatuře se zdá, že struktura 1:1 komplexu se mění v závislosti na původu nebo primární sekvenci cytochromu b5.

Citovat

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.

@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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