Photoaffinity labeling of an antimycin-binding site in Rhodopseudomonas sphaeroides. Academic Article

abstract

• Tritium-labeled 3-azidosalicyl-N-(n-octadecyl)amide was synthesized and used as a photoaffinity probe for the antimycin-binding site in both purified ubiquinone-cytochrome b-c1 oxidoreductase and chromatophore vesicles from the photosynthetic bacterium Rhodopseudomonas sphaeroides. In both systems, a prominently labeled protein had a molecular weight of 11,000. Binding to this protein was inhibited by preincubation of the reaction mixture with antimycin prior to addition of the radioactive analog and subsequent irradiation. The antimycin analog, 3-azidosalicyl-N-(n-octadecyl)amide, inhibited succinate-cytochrome c reductase activity in chromatophore vesicles by 50% at a concentration of 150 nmols/mg of protein.

authors

• Wilson, Emily

published proceedings

• J Biol Chem

author list (cited authors)

• Wilson, E., Farley, T. M., & Takemoto, J. Y.

citation count

• 24

complete list of authors

• Wilson, E||Farley, TM||Takemoto, JY

publication date

• January 1985

publisher

• Elsevier  Publisher

published in

• Journal of Biological Chemistry  Journal

keywords

• Affinity Labels
• Antimycin A
• Azides
• Bacterial Chromatophores
• Binding Sites
• Electron Transport Complex III
• Molecular Weight
• Multienzyme Complexes
• Quinone Reductases
• Rhodobacter Sphaeroides
• Succinate Cytochrome C Oxidoreductase

Digital Object Identifier (DOI)

• 10.1016/s0021-9258(17)39245-1

start page

• 10288

end page

• 10292

volume

• 260

issue

• 18

URL

• http://dx.doi.org/10.1016/s0021-9258(17)39245-1