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cytochrome
(redirected from Cytochrome b5 reductase)

   Also found in: Dictionary/thesaurus, Acronyms, Encyclopedia, Wikipedia, Hutchinson 0.04 sec.
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.
cy·to·chrome (st-krm)
n.
Any of a class of iron-containing proteins important in cell respiration as catalysts of oxidation-reduction reactions.

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

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 exudative electron transport systems associated with adenosine triphosphate production.

cytochrome (sī´tkrōm´),
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.


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Finally, polymorphisms in the activity of cytochrome b5 reductase may mediate the effect of ingested nitrate or endogenously produced nitrite (Gupta et al.
2+]) state again through reductase-mediated electron transfer involving electrons contributed by NADH (reduced diphosphopyridine nucleotide) and cytochrome b5 reductase (methemoglobin reductase), which reduces the methemoglobin (8,10,11).
 
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