Kinetic characterization of cytochrome c oxidase from Bacillus subtilis.
Kinetic characterization of cytochrome c oxidase from Bacillus subtilis.
复制标题
枯草芽孢杆菌细胞色素 C 氧化酶的动力学特征。
DOI:
10.1111/j.1432-1033.1987.tb13553.x
复制
发表时间:
1987
期刊:
影响因子:
--
通讯作者:
W. Konings
中科院分区:
文献类型:
--
作者:
W. Vrij;W. Konings
Bacillus subtilis aa3-type cytochrome c oxidase is capable of oxidizing cytochrome c from different origins. The kinetic properties of the enzyme are influenced by ionic strength. The affinity for Saccharomyces cerevisiae cytochrome c declines with increasing ionic strength whereas the Vmax remains almost constant. An increase of Vmax is observed when the enzyme is incorporated in artificial membranes. Negatively charged phospholipids allow high turnover rates of the aa3-type oxidase. The effect of ionic strength on oxidation of horse heart cytochrome c results in significant changes of both Km and Vmax. These effects can be explained by disturbances of enzyme-substrate interactions and are not related to changes in the aggregation state of the enzyme. The respiration control index of the enzyme reconstituted in artificial membranes appeared to be dependent on phospholipid composition, protein/lipid ratios and also on the external pH. The action of the ionophores nigericin and valinomycin, at various pH values, on the enzyme activity and proton-permeability measurements of the membranes indicate that both components of the proton-motive force, the membrane potential and the pH gradient, can in principle regulate enzyme activity in the reconstituted state.
DOI:
10.1016/s0021-9258(18)34936-6
发表时间:
1982-03
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
W E Jacobus;R W Moreadith;K M Vandegaer
通讯作者:
W E Jacobus;R W Moreadith;K M Vandegaer
DOI:
10.1111/j.1432-1033.1982.tb06667.x
发表时间:
1982
期刊:
European journal of biochemistry
影响因子:
--
作者:
Gennis,RB;Casey,RP;Azzi,A;Ludwig,B
通讯作者:
Ludwig,B
DOI:
--
发表时间:
1984
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Yoshida,T;Fee,JA
通讯作者:
Fee,JA