Abstract
As originally pointed out by Keilin and Hartree (1939), to whom we owe most of the basic definitions in this general field, cytochrome b can be distinguished from the other cytochromes of the respiratory chain, i.e., c and aa 3, on the basis of the following characteristic properties: an oxidation reduction potential permitting its ready reduction by succinate in the presence of the respiratory chain, or chemically by ascorbate, and its oxidation by cytochrome c., an absorption spectrum with its α-, β-, and γ-bands centered around 564, 530, and 432 nm, respectively, and a lack of reaction with typical heme ligands such as CN−. The reported CN−-insensitive oxidation by O2 of the reduced form of the non-covalently attached heme (ferro-protoporphyrin IX) prosthetic group is now known not to be a property of membrane-bound cytochrome b. Since then, a large number of additional cytochromes of the b type (cytochromes B) have been discovered in animal, plant, fungal, and bacterial cells and given rise to a bewildering array of both trivial (i.e., cytochromes b 1,b 2,...b 6) and systematic (e.g., cytochromes b-556, b 556, b-558, or b 558, and b-562 or b 562 of E. coli) designations. The discussion in this essay will be restricted to the classical form of cytochrome b tightly associated with the inner membrane of animal and fungal mitochondria, where it contributes to two segments of their respiratory chain (see below); about 80% of the cytochrome forms part of ubiquinol-cytochrome c reductase (complex III) and the remainder is associated with succinate-cytochrome c reductase (complex II). The reader is referred to a recent review (von Jagow and Sebald, 1980) for a discussion of nonmitochondrial and bacterial cytochromes of the b type and to an article by Bowyer and Trumpower (1981a,b) for a comparison of the mitochondrial bc 1 complex with a similar entity found in photosynthetic bacteria.
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References
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Mahler, H.R., Perlman, P.S. (1985). Cytochrome b of the Respiratory Chain. In: Martonosi, A.N. (eds) The Enzymes of Biological Membranes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4604-3_6
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