细胞色素（Cytochrome）.doc

细胞色素（Cytochrome） Cytochrome A class of electron transfer proteins with iron porphyrin (or heme) as a prosthetic group, widely involved in redox reactions of plants and animals, yeasts, and aerobic bacteria and anaerobic photosynthetic bacteria. Cytochrome as electron carriers of electron transfer is reduced by the heme iron atom (Fe2+) and oxidized (Di) reversible change between. In four the porphyrin ring connected with the iron atom valence bond, the formation of four ligand chelate complexes, commonly called heme. Depending on the structure of the heme cofactor, cytochrome can be divided into a, B, C and D. B cytochrome cofactor is heme iron protoporphyrin IX. The side chain substituents on the porphyrin ring are 4 methyl groups, the two vinyl groups and the two propionic groups are the same as those of the hemoglobin and myoglobin subunits. The structure of a cytochrome cofactor is heme A and heme is in the eighth position of the porphyrin ring to replace the formyl methyl, second with hydroxyl generation farnesene instead of vinyl radical. Cytochrome D is found only in bacteria, and its prosthetic base is iron two hydrogen porphyrin, unlike other cytochromes. The coenzyme group of the class C cytochrome is heme bound covalently with the thiol bonds attached to the vinyl group of its porphyrin ring and cysteine thiol groups in the protein molecule (see Fig.). Other types of cytochromes prosthetic groups are covalently bound to proteins. A characteristic band of light in the visible region: alpha, beta, and gamma bands (or absorption bands). Usually a cytochrome alpha absorption band located at 598 ~ 605 nm; the maximum alpha class B absorption band at 556 nm to 564 nm; C in 550 ~ 555 nm; between the D class is 600 ~ 620 nm. Eukaryotic cells (animal, plant, yeast, Neurospora) oxidative phosphorylation electron transport chain cytoplasmic membrane and mitochondrial membrane of some bacteria in the B, C1, C, a and A3 five kinds of cytochrome. Their redox potential