Cytochrome - Wikipedia
Several kinds of cytochrome exist and can be distinguished by spectroscopy, exact structure of the heme group, inhibitor sensitivity, and reduction potential. [9] Four types of cytochromes are distinguished by their prosthetic groups:
Cytochromes - SpringerLink
Cytochromes are proteins containing one or more heme groups that are involved in electron transfer. The term cytochrome was first coined by David Keilin (1925) to describe a set of intracellular heme-binding proteins that display redox activity with the formation of intense absorption bands between 510 and 615 nm upon reduction.
Cytochrome C - Chemistry LibreTexts
Full Length Ribbon Structure of Cytochrome C (PDB 3cyt). 3 This is the biological assembly of one cytochrome c monomer. Within the central heme is an iron ion shown in orange. The heme is covalently bonded to the protein via disulfide bonds made possible by the recurring Cys-X-Y-Cys-His motif found in cytochromes.
Cytochrome | Protein, Enzyme, Oxidase | Britannica
cytochrome, any of a group of hemoprotein cell components that, by readily undergoing reduction and oxidation (gain and loss of electrons) with the aid of enzymes, serve a vital function in the transfer of energy within cells. Hemoproteins are proteins …
Cytochrome - an overview | ScienceDirect Topics
At present, cytochromes are classified into four types—A, B, C, and D—on the basis of the kind of the heme that they possess as the prosthetic group; A-type cytochrome or cytochrome A has heme a as the prosthetic group, cytochrome B protoheme IX, cytochrome C heme c, and cytochrome D heme d. Cytochrome mainly participates in the energy ...
Cytochrome P450: Structure, Mechanism, and Biochemistry
Volume 1 begins with an exploration of the biophysics and mechanistic enzymology of cytochrome P450 enzymes, with a discussion of the structures of P450 enzymes and their electron donor partners, the mechanisms of oxygen activation and substrate oxidation, and the approaches and nature of cytochrome P450 inhibition.
Cytochromes c: Evolutionary, Structural and Physicochemical …
Cytochromes c are haemoproteins which carry out electron transfer in a wide variety of biological systems, necessitating different kinds of cytochrome c to fulfill different biological roles. The evolutionary relationship between cytochromes c and their host organisms are described, as well as their structural, spectroscopic and redox ...
Cytochrome c - Proteopedia, life in 3D
The structure and function of the cytochrome c2: reaction center electron transfer complex from Rhodobacter sphaeroides. Photosynth Res. 2005;85(1):101-14. PMID: 15977062 doi: 10.1007/s11120-005-1368-8
Cytochrome C - an overview | ScienceDirect Topics
Cytochrome c is a small, water-soluble protein of molecular weight about 12,000. It is a peripheral membrane protein since it can be readily stripped (without detergent) from mitochondrial membranes where it is found. Cytochrome c is associated with specific binding sites on integral membrane proteins extending from the membrane surface.
Cytochrome c : functions beyond respiration - Nature
Cytochrome c is one of the mitochondrial proteins that is released into the cytosol when the cell is activated by an apoptotic stimulus. In the cytosol, cytochrome c engages the apoptotic...