Cytochromes comparative biochemistry

Livingstone, D.R. and Stegeman, J.J. (Eds.) (1998). Forms and Functions of Cytochrome P450. Comparative Biochemistry and Physiology 121C (special issue), 1 12. 

Oya, H., Costello, L.C. and Smith, W.N. (1963) The comparative biochemistry of developing Ascaris eggs. II. Changes in cytochrome c oxidase activity during embryonation. Journal for Cellular and Comparative Physiology 62, 287—294. 

Perkins E. and D. Schlenk (1998). Immunochemical characterization on hepatic cytochrome P450 isozymes in the channel catfish Assessment of sexual, development and treatment-related effects. Comparative Biochemistry and Physiology C 121 305-310. 

Comparative biochemistry. Some researchers believe that the proper role of comparative biochemistry is to put evolution on a molecular basis, and that detoxication enzymes, like other enzymes, are suitable subjects for study. Xenobiotic-metabolizing enzymes were probably essential in the early stages of animal evolution because secondary plant products, even those of low toxicity, are frequently lipophilic and as a consequence would, in the absence of such enzymes, accumulate in lipid membranes and lipid depots. The evolution of cytochrome P450 isoforms, with more than 2000 isoform cDNA sequences known, is proving a useful tool for the study of biochemical evolution. 

Freed, G. (1965). Changes in activity of cytochrome oxidase during adaptation of goldfish to different temperatures. Comparative Biochemistry and Physiology 14,651-665. 

Purification and properties of Moniezia cytochrome c550. Comparative Biochemistry and Physiology, 51B 41-5. 

Kim, Y. Fioravanti, C. F. (1985). Reduction and oxidation of cytochrome c by Hymenolepis diminuta (Cestoda) mitochondria. Comparative Biochemistry and Physiology, 81B 335-9. 

Achazi, R.K., Flenner, C., Livingstone, D.R., Peters, L.D., Schaub, K. and Scheiwe, E. (1998) Cytochrome P450 and dependent activities in unexposed and PAH-exposed terrestrial annelids. Comparative Biochemistry and Physiology B, 121, 339-350. 

Davydov, D.R., Kariakin, A.A., Petushkova, N.A. and Peterson, J.A. (2000) Association of cytochromes P450 with their reductases opposite sign of the electrostatic interactions in P450BM-3 as compared with the microsomal 2B4 system. Biochemistry, 39 (21), 6489-6497. 

Marques-Soares C, Dijols S, Macherey AC, Wester MR, Johnson EF, Dansette PM, Mansuy D. Sulfaphenazole derivatives as tools for comparing cytochrome P450 2C5 and human cytochromes P450 2Cs Identification of a new high affinity substrate common to those enzymes. Biochemistry 2003 42 6363-9. 

Waxman, D.J. (1986). Rat hepatic cytochrome P450 Comparative study of multiple isozymic forms. In P.R. Ortiz de Montellano (ed.), Cytochrome P-450. Structure, Mechanism, and Biochemistry. Plenum Press, New York, NY, pp. 525-538. 

Cytochrome c (see 2 and Fig. 2-7) in the mitochondria is part of the chain of electron carrier proteins that ultimately produce ATP from ADP (oxidative phosphorylation). In principle, the heme in cytochrome c is the same as that in hemoglobin. But in detail, the vinyl groups, after conversion to thioethers, are covalently linked to cysteine amino residues of the protein chain [2,5]. The fifth coordination site of iron is occupied again by the imidazole N-atom of a histidine, but the sixth position is now coordinated to the S-atom of a methionine (Figs. 2-7, 2-17). The redox potential of low-spin Fe(III)/Fe(II) with E°= +0.25 V vs. NHE is drastically altered compared to heme. Now this heme iron is much more able to act in the electron-transporting chain by redox cycling. The mechanisms of electron transfer are available in modem textbooks of biochemistry. It is interesting to note that the macromolecular protein chain... 

Zhao B, Lamb DC, Lei L, Kelly SL, Yuan H, Hachey DL, Waterman MR (2007) Different binding modes of two flaviolin substrate molecules in cytochrome P450 158A1 (CYP158A1) compared to CYP158A2. Biochemistry 46 8725-8733... 

---