Manganese cytochrome c. Structure and properties.
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 کاملCytochrome c oxidase: structure and spectroscopy.
Cytochrome c oxidase, the terminal enzyme of the respiratory chains of mitochondria and aerobic bacteria, catalyzes electron transfer from cytochrome c to molecular oxygen, reducing the latter to water. Electron transfer is coupled to proton translocation across the membrane, resulting in a proton and charge gradient that is then employed by the F0F1-ATPase to synthesize ATP. Over the last year...
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 کاملThe crystal structure of cytochrome c peroxidase.
The three-dimensional conformation of yeast cytochrome c peroxidase has been determined from a 2.5 A electron density map computed with phases obtained from two isomorphous mercury derivatives. Partial sequence information that has recently become available aided in completion of the tracing of the polypeptide backbone, confirmed the presence of a proximal histidine heme ligand and aided in ide...
متن کاملCrystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link.
A specific covalently cross-linked complex between redox partners yeast cytochrome c peroxidase (CCP) and cytochrome c (cyt. c) has been made by engineering cysteines into CCP and cyt. c that form an intermolecular disulfide bond in high yield. The crystal structure of the cross-linked complex has been solved to 1.88-A resolution and closely resembles the structure of the noncovalent complex [P...
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: Journal of Biological Chemistry
سال: 1977
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)40044-5