TY - JOUR
T1 - The cytochrome c binding site on cytochrome c oxidase
AU - Seiter, C. H.A.
AU - Margalit, R.
AU - Perreault, R. A.
N1 - Funding Information:
We thank Dr. M.D. Kamen for helpful discussions, and gratefully acknowledge the assistance of S.G. Angelos, Jr. and Ms. M.C. Navarro. This work was supported by NIH grant 19392, American Chemical Society grant PRF-119G6 and Research Corporation grant RC76.
PY - 1979/2/14
Y1 - 1979/2/14
N2 - Cytochrome c was chemically coupled to cytochrome c oxidase using the reagent 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) which couples amine groups to carboxyl residues. The products of this reaction were analyzed on 2.5-27% polyacrylamide gradient gels electrophoretically. Since cytochrome c binds to cytochrome oxidase electrostatically in an attraction between certain of its lysine residues and carboxyl residues on the oxidase surface, EDC is an especially appropriate reagent probe for binding-subunit studies. Coupling of polylysine to cytochrome oxidase using EDC was also performed, and the products of this reaction indicate that polylysine, an inhibitor of the cytochrome c reaction with oxidase, binds to the same oxidase subunit as does cytochrome c, subunit IV in the gel system used.
AB - Cytochrome c was chemically coupled to cytochrome c oxidase using the reagent 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) which couples amine groups to carboxyl residues. The products of this reaction were analyzed on 2.5-27% polyacrylamide gradient gels electrophoretically. Since cytochrome c binds to cytochrome oxidase electrostatically in an attraction between certain of its lysine residues and carboxyl residues on the oxidase surface, EDC is an especially appropriate reagent probe for binding-subunit studies. Coupling of polylysine to cytochrome oxidase using EDC was also performed, and the products of this reaction indicate that polylysine, an inhibitor of the cytochrome c reaction with oxidase, binds to the same oxidase subunit as does cytochrome c, subunit IV in the gel system used.
UR - http://www.scopus.com/inward/record.url?scp=0018789815&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(79)91738-8
DO - 10.1016/0006-291X(79)91738-8
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AN - SCOPUS:0018789815
SN - 0006-291X
VL - 86
SP - 473
EP - 477
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -