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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 ...
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.
Water softening is the removal of calcium, magnesium, and certain other metal cations in hard water. The resulting soft water requires less soap for the same cleaning effort, as soap is not wasted bonding with calcium ions. Soft water also extends the lifetime of plumbing by reducing or eliminating scale build-up in pipes
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The mobile water-soluble electron carrier is cytochrome c 6 in cyanobacteria, having been replaced by plastocyanin in plants.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