PMID: 168919Aug 11, 1975

Studies on the mechanism of electron transport in the bc1-segment of the respiratory chain in yeast. II. The binding of antimycin to mitochondrial particles and the function of two different binding sites

Biochimica Et Biophysica Acta
G BurgerF Kaudewitz

Abstract

1. In mitochondrial particles antimycin binds to two separate specific sites with dissociation constants KD1 less than 4 - 10(-13) M and KD2 = 3 - 10(-9) M, respectively. 2. The concentrations of the two antimycin binding sites are about equal. The absolute concentration for each binding site is about 100 - 150 pmol per mg of mitochondrial protein. 3. Antimycin bound to the stronger site mainly inhibits NADH-and succinate oxidase. Binding of antimycin to the weaker binding site inhibits the electron flux to exogenously added cytochrome c after blocking cytochrome oxidase by KCN. 4. Under certain conditions cytochrome b and c1 are dispensible components for antimycin-sensitive electron transport. 5. A model of the respiratory chain in yeast is proposed which accounts for the results reported here and previously. (Lang, B., Burger, G., and Bandlow, W. (1974) Biochim. Biophys. Acta 368, 71-85).

References

Apr 27, 1973·Biochimica Et Biophysica Acta·C J Grimmelikhuijzen, E C Slater
Dec 14, 1972·Biochimica Et Biophysica Acta·M K Wikström, J A Berden
Mar 26, 1974·Biochimica Et Biophysica Acta·W BandlowE C Slater
Jan 1, 1974·Molecular & General Genetics : MGG·W Bandlow, F Kaudewitz
Feb 28, 1972·Biochimica Et Biophysica Acta·J A Berden, E C Slater

Related Concepts

Antimycin A1
Cochliobolus
Isocyanides
Cytochrome c Oxidase Subunit VIa
Cytochromes
Respiratory Chain
Mitochondria
NADH, NADPH Oxidoreductases
Oxygen Consumption
Plasma Protein Binding Capacity

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