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- W137644832 abstract "This chapter focuses on functional limits of cytochrome c variability. Cytochrome c is the protein for which the primary structure is known for the largest number of species and covering the complete taxonomic scale. Though some seventy residue positions have been occupied by different amino acids in the cytochromes c of all the species so far examined, it can be demonstrated, for example, that on the average no more than about ten of these residues are amenable to evolutionary change in the cytochrome c of any one mammalian species. The amino-acid sequences of the proteins employed in deriving a tree are compared in terms of so-called minimal replacement distances, namely, the minimal number of single nucleotide changes required to transform the gene coding for one into the gene coding for another. In terms of their electron transport ability and their ability to sustain oxidative phosphorylation in mitochondria, as well as their reaction with preparations of cytochrome c oxidase, all cytochromes c tested so far have failed to reveal any differences whatsoever." @default.
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- W137644832 date "1972-01-01" @default.
- W137644832 modified "2023-09-23" @default.
- W137644832 title "FUNCTIONAL LIMITS OF CYTOCHROME c VARIABILITY" @default.
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- W137644832 doi "https://doi.org/10.1016/b978-0-08-016874-6.50007-2" @default.
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