Physicochemical properties of two atypical cytochromes c, Crithidia cytochrome c-557 and Euglena cytochrome c-558
نویسندگان
چکیده
منابع مشابه
Physicochemical properties of two atypical cytochromes c, Crithidia cytochrome c-557 and Euglena cytochrome c-558.
Cytochrome c-557 from Crithidia oncopelti and cytochrome c-558 from Euglena gracilis are mitochondrial cytochromes c that have an atypical haem-binding site. It was of interest to know whether the loss of one thioether bond affected the physicochemical properties of these cytochromes. The thermodynamic parameters of the redox potential were measured. The reaction with imidazole, the kinetics an...
متن کاملHomology of Pseudomonas cytochrome c-551 with eukaryotic c-cytochromes.
The homology of Pseudomonas cytochrome c-551 with eukaryotic cytochromes c is examined with a computer-based procedure devised to determine whether similarities exist between these proteins. One method is given by which the more recently evolved cytochromes c might have arisen from the Pseudomonas protein. This procedure involves only common genetic phenomena and accounts for most of the struct...
متن کاملTwo c-type cytochromes from light- and dark-grown Euglena.
A pigment-protein complex can be extracted, in aqueous 2-percent digitonin, from Euglena grown in the light. When further fractionated by acetone and ammonium sulfate this flagellate yields a c-type cytochrome. By similar extraction of dark-grown, nonphotosynthetic Euglena, another c-type cytochrome can be isolated. The cytochrome from the light-grown Euglena- is like that of cytochrome c isola...
متن کاملCytochrome c
How is it made? Cytochrome c is synthesized from two inactive precursor molecules: apocytochrome c (a protein that is encoded by a nuclear gene and imported into mitochondria) and heme (which is synthesized in mitochondria). The covalent attachment of apocytochrome c to heme is catalyzed by heme lyase and creates cytochrome c, a 14.5 kDa protein that is normally confined to the intermembrane sp...
متن کاملConformational properties of cardiolipin-bound cytochrome c.
Interactions of cytochrome c (cyt c) with cardiolipin (CL) are important for both electron transfer and apoptotic functions of this protein. A sluggish peroxidase in its native state, when bound to CL, cyt c catalyzes CL peroxidation, which contributes to the protein apoptotic release. The heterogeneous CL-bound cyt c ensemble is difficult to characterize with traditional structural methods and...
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: Biochemical Journal
سال: 1975
ISSN: 0264-6021
DOI: 10.1042/bj1490155