cytochrome


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cytochrome

 [si´to-krōm]
any of a class of hemoproteins, widely distributed in animal and plant tissue, whose main function is electron transport; distinguished according to their non–amino acid components as a, b, c, d, etc.

cy·to·chrome

(sī'tō-krōm),
A class of hemoprotein the principal biologic function of which is electron and/or hydrogen transport by virtue of a reversible valency change of the heme iron. Cytochromes are classified in four groups (a, b, c, and d) according to spectrochemical characteristics; many variants exist, particularly among bacteria and in green plants and algae, one being a variant of the c type cytochrome called cytochrome f. The mitochondrial system of cytochromes provides electron transport through cytochrome c oxidase to molecular oxygen as the terminal electron acceptor (respiration).
[cyto- + G. chrōma, color]

cytochrome

(sī′tə-krōm′)
n.
Any of a class of usually colored proteins that contain a heme group, are electron carriers, and catalyze oxidation-reduction reactions during cellular respiration.

cy·to·chrome

(sī'tō-krōm)
A class of hemoprotein the principal biologic function of which is electron or hydrogen transport by virtue of a reversible valency change of the heme iron. Many variants exist, particularly among bacteria and in green plants and algae, one being a variant of the c type cytochrome called cytochrome f. The mitochondrial system of cytochromes provides electron transport through cytochrome c oxidase to molecular oxygen as the terminal electron acceptor (respiration).
[cyto- + G. chrōma, color]

cytochrome

a protein pigment containing iron that is capable of being alternately oxidized and reduced, acting as an electron carrier in, for example, the ELECTRON TRANSPORT SYSTEM of a MITOCHONDRION.

Cytochrome

A substance that contains iron and acts as a hydrogen carrier for the eventual release of energy in aerobic respiration.
Mentioned in: Smoking

cy·to·chrome

(sī'tō-krōm)
A class of hemoprotein the principal biologic function of which is electron or hydrogen transport.
[cyto- + G. chrōma, color]
References in periodicals archive ?
Table 1: Nuclear-encoded cytochrome c oxidase subunit isoform mutations (1).
Gelboin, "Analysis of human cytochrome P450 catalytic activities and expression," The Tohoku Journal of Experimental Medicine, vol.
Genetic polymorphisms of Cytochrome P450 2D6 (CYP2D6): clinical consequences, evolutionary aspects and functional diversity.
The aims of present study were compare the morphometric data between left and right adrenal of males and females; perform a histological, scanning and transmission electron microscopy study showing tissue constitution of glands; finally, in order to define the presence and correct site of the cytochrome P450c17 expression in adrenal glands, immunohistochemical study of this enzyme was performed.
On the other hand T2 target protein was found to interact with cbb3-type cytochrome c oxidase subunit II (ccoO) involved in the transfer of electron from cytochrome c to catalytic subunit I and ubiquinol-cytochrome C reductase cytochrome B subunit (petB) involved in ATP generation (Table 6).
Villard et al., "Cytochrome P450 2C19 loss-of-function polymorphism is a major determinant of clopidogrel responsiveness in healthy subjects," Blood, vol.
Expression of AIF, cytochrome c, Bax, Bcl-xl, LC3B-I/II and p62 was detected by western blotting using routine method.
Permethrin induction of multiple cytochrome P450 genes in insecticide resistant mosquitoes, Culex quinquefasciatus.
Cytochrome P-450 dependent mono oxygenases are a very diverse group of heme containing hydrophobic enzymes that involve in detoxification of various exogenous and endogenous compounds.
Cytochrome b gene for species identification of the conservation animals.
Interaction of cytochrome P450 3A inhibitors with P-glycoprotein.