Interaction of cytochrome c with cytochrome oxidase:: two different docking scenarios

被引:72
作者
Maneg, O
Malatesta, F
Ludwig, B
Drosou, V
机构
[1] Univ Frankfurt, Inst Biochem, Biozentrum N200, D-60439 Frankfurt, Germany
[2] Univ Aquila, Dept Pure & Appl Biol, Laquila, Italy
[3] Aventis Pharma Deutschland GMBH, Frankfurt, Germany
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2004年 / 1655卷 / 1-3期
关键词
electrostatic interaction; docking complex; electron transfer; Cu-A center; Paracoccus denitrificans; Thermus thermophilus;
D O I
10.1016/j.bbabio.2003.10.010
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cytochrome c is the specific and efficient electron transfer mediator between the two last redox complexes of the mitochondrial respiratory chain. Its interaction with both partner proteins, namely cytochrome c(1) (of complex III) and the hydrophilic Cu-A domain (of subunit II of oxidase), is transient, and known to be guided mainly by electrostatic interactions, with a set of acidic residues oil the presumed docking site on the Cu-A domain surface and a complementary region of opposite charges exposed on cytochrome c. Information from recent structure determinations of oxidases from both mitochondria and bacteria, site-directed mutagenesis approaches, kinetic data obtained from the analysis of isolated soluble modules of interacting redox partners, and computational approaches have yielded new insights into the docking and electron transfer mechanisms. Here, we summarize and discuss recent results obtained from bacterial cytochrome c oxidases from both Paracoccus denitrificans, in which the primary electrostatic encounter most closely matches the mitochondrial situation, and the Thermus thermophilus ba(3) oxidase in which docking and electron transfer is predominantly based on hydrophobic interactions. (C) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码:274 / 281
页数:8
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