Structural and functional organization of Complex I in the mitochondrial respiratory chain

被引：43

作者：

Bianchi, C ^{[1
]}

Fato, R ^{[1
]}

Genova, ML ^{[1
]}

Castelli, GP ^{[1
]}

Lenaz, G ^{[1
]}

机构：

[1] Univ Bologna, Dipartimento Biochim G Moruzzi, I-40126 Bologna, Italy

来源：

BIOFACTORS | 2003年 / 18卷 / 1-4期

关键词：

mitochondria; coenzyme Q pool; supercomplex; flux control; complex I; complex III;

D O I：

10.1002/biof.5520180202

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：

Metabolic flux control analysis of NADH oxidation in bovine heart submitochondrial particles revealed high flux control coefficients for both Complex I and Complex III, suggesting that the two enzymes are functionally associated as a single enzyme, with channelling of the common substrate, Coenzyme Q. This is in contrast with the more accepted view of a mobile diffusable Coenzyme Q pool between these enzymes. Dilution with phospholipids of a mitochondrial fraction enriched in Complexes I and III, with consequent increased theoretical distance between complexes, determines adherence to pool behavior for Coenzyme Q, but only at dilution higher than 1:5 (protein: phospholipids), whereas, at lower phospholipid content, the turnover of NADH cytochrome c reductase is higher than expected by the pool equation.

引用

页码：3 / 9

页数：7

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