固定在脂质双层膜内的细胞色素c氧化酶电化学研究_英文_.docVIP

第7 卷 第6 期 石家庄学院学报 Vol.7，No.6 2005 年11 月 Journal of Shijiazhuang College Nov.2005 Electr ochemical Study on Cytochr ome C O xida se I m m ob ilized into L ipid Bilayer Membr ane SU Lian- yong （Department of Chemistry, Virginia Commonwealth University, Richmond, VA 23284- 2006, USA） Abstract：Lipid bilayer membrane containing monomeric bovine cytochrome c oxidase was successfully immobilized in gold quartz crystal microbalance electrodes. Direct electron transfer on the oxidase modified electrode was observed over a wide range of pH, temperature and buffer concentration. The oxidase modified electrode maintains direct electron transfer properties at the temperature in excess of 80 °C. Upon cooling down the electrode to room temperature, the oxidase still retained its electron transfer capabilities. Temperature can cause phase transition of cytochrome c oxidase in the temperature range of 22 to 80 °C. The corresponding reaction activation energies before and after the transition were estimated. Acetonitrile binding to cytochrome c oxidase during the electroxidative process of solution- resident ferrocytochrome c was also investigated by flow injection analysis. The results showed that cytochrome c oxidase forms a complex with acetonitrile having a Ki of 1.3 M with a stoichiometry of 1 acetonitrile molecule per cytochrome c oxidase. The binding of acetonitrile to cytochrome oxidase is a reversible process. Key words:Direct electron transfer；cytochrome c oxidase；lipid bilayer membrane；Cytochrome c CLC number：O646 Document code：A Article ID：1673- 197（2 2005）06- 0005- 08 1 Introduction The cytochrome c oxidases， along with other members of the superfamily of“heme - copper oxidases”, are responsible for nearly all- aerobic respiration on earth[1，2]. Cytochrome c oxidase reduces dioxygen to water in a way that conserves the considerable free energy made available from this highly favorable reaction. This free energy is used for a wide variety of energy- requiring biological