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Cytochrome c is a highly conserved protein across the spectrum of eukaryotic species, found in plants, animals, fungi, and many unicellular organisms. This, along with its small size (molecular weight about 12,000 daltons), [7] makes it useful in studies of cladistics. [8]
Small soluble cytochrome c proteins with a molecular weight of 8-12 kDa and a single heme group belong to class I. [10] [11] It includes the low-spin soluble cytC of mitochondria and bacteria, with the heme-attachment site located towards the N-terminus, and the sixth ligand provided by a methionine residue about 40 residues further on towards the C-terminus.
There is no "cytochrome e," but cytochrome f, found in the cytochrome b 6 f complex of plants is a c-type cytochrome. [12] In mitochondria and chloroplasts, these cytochromes are often combined in electron transport and related metabolic pathways: [13]
The enzyme cytochrome c oxidase or Complex IV (was EC 1.9.3.1, now reclassified as a translocase EC 7.1.1.9) is a large transmembrane protein complex found in bacteria, archaea, and the mitochondria of eukaryotes.
The mobile cytochrome electron carrier in mitochondria is cytochrome c. Bacteria use a number of different mobile cytochrome electron carriers. Other cytochromes are found within macromolecules such as Complex III and Complex IV. They also function as electron carriers, but in a very different, intramolecular, solid-state environment.
In mitochondria, it is found in cytochrome c oxidase, which is the last protein in oxidative phosphorylation. Cytochrome c oxidase is the protein that binds the O 2 between a copper and an iron; the protein transfers 4 electrons to the O 2 molecule to reduce it to two molecules of water.
The Food and Drug Administration (FDA) has revoked the use of Red Dye No. 3 (also known as erythrosine, Red Dye 3, FD&C Red No. 3 and Red No. 3) in food and ingested drugs as of January 15 ...
The redox potential for cytochrome c can also be "fine-tuned" by small changes in protein structure and solvent interaction. [4] The number of heme C units bound to a holoprotein is highly variable. For vertebrate cells one heme C per protein is the rule but for bacteria this number is often 2, 4, 5, 6 or even 16 heme C groups per holoprotein.