S15.14 Stochastic approach of bc1 complex functioning
نویسندگان
چکیده
منابع مشابه
Crystallization of cytochrome bc1 complex.
Complex III (cytochrome bc1 particle; ubiquinol:ferricytochrome c oxidoreductase, EC 1.10.2.2) was purified from beef heart mitochondria by a combination of hydrophobic interaction and affinity chromatography. By washing the complex with detergent on the hydrophobic interaction column, phospholipids were effectively depleted; 7 mol of cardiolipin per mol of cytochrome c1 was retained in the fin...
متن کاملBiodiversity and ecosystem functioning: A complex adaptive systems approach
Environmental factors regulate biodiversity through species sorting processes. Species distributions in communities affect ecosystem processes and environmental factors. These dynamics are determined by the properties (traits) of species in the community. The optimal temperatures for growth, the minimal amount of resource that sustains positive mass balance, and the amount of energy allocated t...
متن کاملThe cytochrome bc1 complex: function in the context of structure.
The bc1 complexes are intrinsic membrane proteins that catalyze the oxidation of ubihydroquinone and the reduction of cytochrome c in mitochondrial respiratory chains and bacterial photosynthetic and respiratory chains. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. Genetic defects leading to mu...
متن کاملProtonmotive pathways and mechanisms in the cytochrome bc1 complex.
The cytochrome bc(1) complex catalyzes electron transfer from ubiquinol to cytochrome c by a protonmotive Q cycle mechanism in which electron transfer is linked to proton translocation across the inner mitochondrial membrane. In the Q cycle mechanism proton translocation is the net result of topographically segregated reduction of quinone and reoxidation of quinol on opposite sides of the membr...
متن کاملSuperoxide anion generation by the cytochrome bc1 complex.
We have measured the rates of superoxide anion generation by cytochrome bc(1) complexes isolated from bovine heart and yeast mitochondria and by cytochrome bc(1) complexes from yeast mutants in which the midpoint potentials of the cytochrome b hemes and the Rieske iron-sulfur cluster were altered by mutations in those proteins. With all of the bc(1) complexes the rate of superoxide anion produc...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 2008
ISSN: 0005-2728
DOI: 10.1016/j.bbabio.2008.05.412