石家庄学院学报
石傢莊學院學報
석가장학원학보
Journal of Shijiazhuang University
2005年
6期
5~12
,共null页
直接电子迁移 细胞色素c氧化酶 脂质双层膜 细胞色素c
直接電子遷移 細胞色素c氧化酶 脂質雙層膜 細胞色素c
직접전자천이 세포색소c양화매 지질쌍층막 세포색소c
Direct electron transfer;cytochrome c oxidase;lipid bilayer membrane;Cytochrome c
含有单体牛细胞色素c氧化酶的脂质双层膜,被成功地固定在金石英晶体微平衡电极上.在较宽的pH值、温度和缓冲浓度范围内观察到了氧化酶修饰电极上的直接电子迁移.氧化酶修饰电极在80℃以上时保持直接电子迁移性质,将电极冷却到室温时,氧化酶仍保持电子迁移能力.在22~80℃范围内,温度变化可引起细胞色素c氧化酶的相转移,估计出了相转移前后的相应反应活化能通过射流分析,研究了在溶液含有亚铁细胞色素c氧化酶的电氧化过程中,乙腈同细胞色素c氧化酶的结合.结果显示:浓度1.3M具有常数Ki时,细胞色素c氧化酶和乙腈形成配合物,每个细胞色素c氧化酶配一个乙腈分子,乙腈同细胞色素氧化酶的结合过程是可逆过程.
含有單體牛細胞色素c氧化酶的脂質雙層膜,被成功地固定在金石英晶體微平衡電極上.在較寬的pH值、溫度和緩遲濃度範圍內觀察到瞭氧化酶脩飾電極上的直接電子遷移.氧化酶脩飾電極在80℃以上時保持直接電子遷移性質,將電極冷卻到室溫時,氧化酶仍保持電子遷移能力.在22~80℃範圍內,溫度變化可引起細胞色素c氧化酶的相轉移,估計齣瞭相轉移前後的相應反應活化能通過射流分析,研究瞭在溶液含有亞鐵細胞色素c氧化酶的電氧化過程中,乙腈同細胞色素c氧化酶的結閤.結果顯示:濃度1.3M具有常數Ki時,細胞色素c氧化酶和乙腈形成配閤物,每箇細胞色素c氧化酶配一箇乙腈分子,乙腈同細胞色素氧化酶的結閤過程是可逆過程.
함유단체우세포색소c양화매적지질쌍층막,피성공지고정재금석영정체미평형전겁상.재교관적pH치、온도화완충농도범위내관찰도료양화매수식전겁상적직접전자천이.양화매수식전겁재80℃이상시보지직접전자천이성질,장전겁냉각도실온시,양화매잉보지전자천이능력.재22~80℃범위내,온도변화가인기세포색소c양화매적상전이,고계출료상전이전후적상응반응활화능통과사류분석,연구료재용액함유아철세포색소c양화매적전양화과정중,을정동세포색소c양화매적결합.결과현시:농도1.3M구유상수Ki시,세포색소c양화매화을정형성배합물,매개세포색소c양화매배일개을정분자,을정동세포색소양화매적결합과정시가역과정.
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℃. 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℃. 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 K; 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.