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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] Cytochrome c has been studied for the glimpse it gives into evolutionary ...
The mobile water-soluble electron carrier is cytochrome c 6 in cyanobacteria, having been replaced by plastocyanin in plants. [8] Cyanobacteria can also synthesize ATP by oxidative phosphorylation, in the manner of other bacteria. The electron transport chain is NADH dehydrogenase → plastoquinol → b 6 f → cyt c 6 → cyt aa 3 → O 2
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.
Complex III itself is composed of several subunits, one of which is a b-type cytochrome while another one is a c-type cytochrome. Both domains are involved in electron transfer within the complex. Complex IV contains a cytochrome a/a3-domain that transfers electrons and catalyzes the reaction of oxygen to water.
The mechanism involves ferrous cytochrome c (Cc) providing electrons for the Cc-CcP system to reduce hydrogen peroxide to water. [4] The complex is formed by non-covalent interactions. [5] Cytochrome c peroxidase can react with hydroperoxides other than hydrogen peroxide, but the reaction rate is much slower than with hydrogen peroxide.
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.
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