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

/cy·to·chrome/ (si´to-krōm) any of a class of hemoproteins, widely distributed in animal and plant tissues, whose main function is electron transport using the heme prosthetic group; distinguished according to their prosthetic groups, e.g., a, b, c, d, and P-450.

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.

cytochrome

[si′tōkrōm]
Etymology: Gk, kytos, cell, chroma, color
1 a class of hemoproteins whose function is electron transport. These proteins have the ability to change the valence of the heme iron, alternating between ferrous and ferric states.
2 proteins involved in mitochondrial electron transport systems associated with adenosine triphosphate (ATP) production.

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]

cytochrome (sī´təkrōm´),

n one of a class of hemoproteins that act as electron transport. Cytochromes are classified as
a, b, c, and
d.

cytochrome

any of a class of hemoproteins, widely distributed in animal and plant tissue, whose main function is electron transport; distinguished according to their prosthetic group as a, b, c and d.

cytochrome b5 reductase
a flavoprotein involved in the desaturation of fatty acids in the liver.
cytochrome oxidase
an a type cytochrome which contains copper and receives electrons from another cytochrome, of the c type, and transfers them to oxygen atoms allowing the oxygen to combine with hydrogen atoms to form water. A nutritional deficiency of copper leads to a general reduction in metabolic rate because of the absence of cytochrome oxidase a.
cytochrome system
the sum of cytochromes which play a part in the body's metabolic processes. Includes the cytochrome oxidases and cytochrome reductases.
References in periodicals archive ?
GB 2 408 509 B covering the use of the crystal structure of human cytochrome P450 3A4 granted on 1st November 2006
Although not included in the labeling of cisapride, ritonavir, the new protease inhibitor, is a potent inhibitor of the cytochrome P450-3A4 enzyme.
However, the Human Genome Project has identified a cohort of extra-hepatic cytochrome P450s that are over-expressed during the malignant progression of most cancers (both solid and hematological malignancies) but not in normal tissue.
Conclusions* The data indicate no or minor potential for herb-drug interactions by interference with cytochromes P450 by any of the three mistletoe extracts.
The resulting WIF-B cell line expressed both alcohol dehydrogenase and cytochrome P450 2E1, maintained polarity, and formed functional bile canaliculi (Shanks et al.
Conversely, there was no difference in expression of cytosolic cytochrome c protein in any of the groups, and there was a significant decrease in active caspase-9 protein level in the medium- and high-dose groups (Figure 4A,B).
John's wort for this purpose stems from the fact that doing so will speed up the metabolism of any other drugs the patient might be taking that are dependent upon the cytochrome P450 3A4 enzyme pathway.
The cytochrome P-450 family contains a wide range of isoenzymes that metabolize over 200,000 substrates (Lewis et al.
Consistently, the mitochondrial cytochrome b gene of this isolate, determined by the methods similar to previous report except the PCR primers (mtPk-F:5'-AGGTATTATATTCTTTATACAAATATTAAC-3' and mtPk-R:5'-TCTTTTATAATGAACAAGTGTAAATAATC-3'), displayed perfect sequence identity with that of P.
Previous studies of single Xenopus oocytes have shown that microinjection of cytochrome c induces apoptotic cell death, accompanied by a progressive loss of membrane potential, activation of caspase 3, and DNA fragmentation (6).