ubiquinol and bathocuproine

ubiquinol has been researched along with bathocuproine* in 1 studies

Other Studies

1 other study(ies) available for ubiquinol and bathocuproine

Article	Year
Essential role of copper in the activity and regular periodicity of a recombinant, tumor-associated, cell surface, growth-related and time-keeping hydroquinone (NADH) oxidase with protein disulfide-thiol interchange activity (ENOX2). Journal of bioenergetics and biomembranes, 2010, Volume: 42, Issue:5 ECTO-NOX proteins are growth-related cell surface proteins that catalyze both hydroquinone or NADH oxidation and protein disulfide interchange and exhibit time-keeping and prion-like properties. A bacterially expressed truncated recombinant 46 kDa ENOX2 with full ENOX2 activity bound ca 2 moles copper and 2 moles of zinc per mole of protein. Unfolding of the protein in trifluoroacetic acid in the presence of the copper chelator bathocuproine resulted in reversible loss of both enzymatic activities and of a characteristic pattern in the Amide I to Amide II ratios determined by FTIR with restoration by added copper. The H546-V-H together with His 562 form one copper binding site and H582 represents a second copper site as determined from site-directed mutagenesis. Bound copper emerges as having an essential role in ENOX2 both for enzymatic activity and for the structural changes that underly the periodic alternations in activity that define the time-keeping cycle of the protein. Topics: Binding Sites; Blotting, Western; Copper; Escherichia coli; Humans; Models, Biological; Mutagenesis, Site-Directed; NAD; NADH, NADPH Oxidoreductases; Oligonucleotides; Oxygen; Periodicity; Phenanthrolines; Protein Disulfide-Isomerases; Spectrophotometry, Infrared; Spectroscopy, Fourier Transform Infrared; Ubiquinone; Zinc	2010

Article

Year

Essential role of copper in the activity and regular periodicity of a recombinant, tumor-associated, cell surface, growth-related and time-keeping hydroquinone (NADH) oxidase with protein disulfide-thiol interchange activity (ENOX2).

Journal of bioenergetics and biomembranes, 2010, Volume: 42, Issue:5

ECTO-NOX proteins are growth-related cell surface proteins that catalyze both hydroquinone or NADH oxidation and protein disulfide interchange and exhibit time-keeping and prion-like properties. A bacterially expressed truncated recombinant 46 kDa ENOX2 with full ENOX2 activity bound ca 2 moles copper and 2 moles of zinc per mole of protein. Unfolding of the protein in trifluoroacetic acid in the presence of the copper chelator bathocuproine resulted in reversible loss of both enzymatic activities and of a characteristic pattern in the Amide I to Amide II ratios determined by FTIR with restoration by added copper. The H546-V-H together with His 562 form one copper binding site and H582 represents a second copper site as determined from site-directed mutagenesis. Bound copper emerges as having an essential role in ENOX2 both for enzymatic activity and for the structural changes that underly the periodic alternations in activity that define the time-keeping cycle of the protein.

Topics: Binding Sites; Blotting, Western; Copper; Escherichia coli; Humans; Models, Biological; Mutagenesis, Site-Directed; NAD; NADH, NADPH Oxidoreductases; Oligonucleotides; Oxygen; Periodicity; Phenanthrolines; Protein Disulfide-Isomerases; Spectrophotometry, Infrared; Spectroscopy, Fourier Transform Infrared; Ubiquinone; Zinc

2010