Cytochrome c release from mitochondria induces caspase activation in cytosols; however, it is unclear whether the redox state of cytosolic cytochrome c can regulate caspase activation. By using cytosol isolated from mammalian cells, we find that oxidation of cytochrome c by added cytochrome oxidase stimulates caspase activation, whereas reduction of cytochrome c by added tetramethylphenylenedia...

normal 0 false false false en-us x-none ar-sa microsoftinternetexplorer4 background : lung cancer has remained the most prevalent malignancy worldwide. it is the fifth leading cause of cancer death in iran. nevertheless, during last few years a gradual permanent increase in its incidence has been reported. although the crucial role of tobacco smoke in lung cancer initiation has long been establ...

cigarette smoking is one of the main risk factors for premature human death associated to a variety of respiratory and vascular diseases, and cancer due to containing hundreds of toxicants. rat mitochondria were obtained by differential ultracentrifugation and incubated with different concentrations (1, 10 and 100%) of standardized cigarette smoke extract (cse). our results showed that cigarett...

The interactions between purified rat hepatic m rosomal cytochrome P-450 and the type I ligands benzphetamine and cytochrome b6 have been studied in the presence of phospholipid using difference spectrophotometry. Cytochrome bs was shown to interact with cytochrome P-450 to form a tight 1:1 complex (Kd = 275 nM), in which the proportion of high spin cytochrome P-450 was increased from 7 to 30%....

Cytochrome cM was first described in 1994 and its sequence has been found the genome of manifold cyanobacterial species ever since. Numerous studies have carried out with purpose determining function, but none them given place to conclusive results so far. Many these are based on assumption that cytochrome is a soluble protein located thylakoid lumen cyanobacteria. In this work, we reevaluated ...

Based on the atomic structures of the mitochondrial cytochrome bc(1) complex, it has been proposed that the soluble domain of the [2Fe-2S] Rieske iron-sulfur protein (ISP) must rotate by ca. 60 degrees and translate through an appreciable distance between two binding sites, proximal to cytochrome c(1) and to the lumen-side quinol binding site. Such motional freedom implies that the electron-tra...