oligomycins and acrylodan

oligomycins has been researched along with acrylodan* in 1 studies

Other Studies

1 other study(ies) available for oligomycins and acrylodan

Article	Year
A fluorescent derivative of the oligomycin-sensitivity conferring protein (acrylodan-OSCP). Evidence for polarity changes in the environment of CYS118 of OSCP upon binding to mitochondrial F1. Biochemical and biophysical research communications, 1987, Jan-15, Volume: 142, Issue:1 The fluorescent probe, 6-acryloyl-2-dimethylaminonaphtalene (acrylodan) was reacted with the oligomycin-sensitivity conferring protein (OSCP). Acrylodan bound covalently to the single cysteinyl residue of the protein. Acrylodan-OSCP was fully competent in conferring oligomycin sensitivity to the mitochondrial F0-F1 ATPase complex. The fluorescence emission peak of acrylodan-OSCP was blue-shifted compared to that of an acrylodan-mercaptoethanol adduct, which means that acrylodan experiences a hydrophobic environment in OSCP. Binding of acrylodan-OSCP to the isolated F1 was accompanied by a red shift of fluorescence. It was achieved in less than 1 s at 25 degrees C. The titration curve revealed one high affinity OSCP binding site per F1. Acrylodan-OSCP appears to be an interesting tool for studying the dynamics of structural changes within the mitochondrial ATPase complex. Topics: 2-Naphthylamine; Adenosine Triphosphatases; Animals; Carrier Proteins; Cattle; Cysteine; Kinetics; Membrane Proteins; Mitochondria, Heart; Mitochondrial Proton-Translocating ATPases; Oligomycins; Proton-Translocating ATPases; Solubility; Spectrometry, Fluorescence	1987

Article

Year

A fluorescent derivative of the oligomycin-sensitivity conferring protein (acrylodan-OSCP). Evidence for polarity changes in the environment of CYS118 of OSCP upon binding to mitochondrial F1.

Biochemical and biophysical research communications, 1987, Jan-15, Volume: 142, Issue:1

The fluorescent probe, 6-acryloyl-2-dimethylaminonaphtalene (acrylodan) was reacted with the oligomycin-sensitivity conferring protein (OSCP). Acrylodan bound covalently to the single cysteinyl residue of the protein. Acrylodan-OSCP was fully competent in conferring oligomycin sensitivity to the mitochondrial F0-F1 ATPase complex. The fluorescence emission peak of acrylodan-OSCP was blue-shifted compared to that of an acrylodan-mercaptoethanol adduct, which means that acrylodan experiences a hydrophobic environment in OSCP. Binding of acrylodan-OSCP to the isolated F1 was accompanied by a red shift of fluorescence. It was achieved in less than 1 s at 25 degrees C. The titration curve revealed one high affinity OSCP binding site per F1. Acrylodan-OSCP appears to be an interesting tool for studying the dynamics of structural changes within the mitochondrial ATPase complex.

Topics: 2-Naphthylamine; Adenosine Triphosphatases; Animals; Carrier Proteins; Cattle; Cysteine; Kinetics; Membrane Proteins; Mitochondria, Heart; Mitochondrial Proton-Translocating ATPases; Oligomycins; Proton-Translocating ATPases; Solubility; Spectrometry, Fluorescence

1987