A study of cytochrome bo(3) in a tethered bilayer lipid membrane

作者：Weiss Sophie A; Bushby Richard J; Evans Stephen D; Jeuken Lars J C^*

来源：Biochimica et Biophysica Acta-Bioenergetics, 2010, 1797(12): 1917-1923.

DOI：10.1016/j.bbabio.2010.01.012

• Ubiquinol oxidase
• Cytochrome c oxidase
• Electrochemistry
• Tethered bilayer lipid membrane
• Enzyme mechanism

An assay has been developed in which the activity of an ubiquinol oxidase from Escherichia coli cytochrome bo(3) (cbo(3)) is determined as a function of the hydrophobic substrate ubiquinol-10 (UQ-10) in tethered bilayer lipid membranes (tBLMs) UQ 10 was added in situ while the enzyme activity and the UQ-10 concentration in the membrane have been determined by cyclic voltammetry Cbo(3) is inhibited by UQ-10 at concentrations above 5-10 pmol/cm(2) while product inhibition is absent Cyclic voltammetry has also been used to characterise the effects of three inhibitors cyanide inhibiting oxygen reduction 2-n-Heptyl-4-hydroxyquinoline N-oxide (HQNO) inhibiting the quinone oxidation and Zn(II) thought to block the proton channels required for oxygen reduction and proton pumping amity The electrochemical behaviour of cbo(3) inhibited with HQNO and Zn(II) is almost identical suggesting that Zn(II) ions inhibit the enzyme reduction by quinol rather than oxygen reduction T

• 出版日期2010-12