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Last modified: 12 January 1999


Reviews on structure and function of cytochrome b5 family

  1. Angelov, E. (1991) Cytochrome b5 - Its molecular characteristics and biochemical significance. Eksp. Med. Morfol. 30, 36-45.
  2. Borgese, N., D'Arrigo, A., De Silvestris, M. and Pietrini, G. (1993a) NADH-cytochrome b5 reductase and cytochrome b5 isoforms as models for the study of post­translational targeting to the endoplasmic reticulum. FEBS Lett. 325, 70-75.
  3. Borgese, N., D'Arrigo, A., De Silvestris, M. and Pietrini, G. (1993b) NADH-cytochrome b5 reductase and cytochrome b5. The problem of posttranslational targeting to the endoplasmic reticulum. Subcell. Biochem. 21, 313-341.
  4. Capeillèere­Blandin, C. (1995) Flavocytochrome b2-cytochrome c interactions: The electron transfer reaction revisited. Biochimie 77, 516-530.
  5. Chapman, S.K., Reid, G.A., Bell, C., Short, D. and Daff, S. (1996) Flavocytochrome b2: An ideal model system for studying protein­mediated electron transfer. Biochem. Soc. Trans. 24, 73-77.
  6. Durham, B., Fairris, J.L., McLean, M., Millett, F., Scott, J.R., Sligar, S.G. and Willie, A. (1995) Electron transfer from cytochrome b5 to cytochrome c. J. Bioenerg. Biomembr. 27, 331-340.
  7. Guiard, B. and Lederer, F. (1978) Surface differences and similarities in two homologous proteins. Cytochrome b5 and cytochrome b2 core. Biochim. Biophys. Acta 536, 88-96.
  8. Guiard, B. and Lederer, F. (1979) The "cytochrome b5 fold": structure of a novel protein superfamily. J. Mol. Biol. 135, 639-650.
  9. Ito, A. (1983) Structure, function and biogenesis of cytochrome b5­families. Seikagaku 55, 145-159.
  10. Lederer, F. (1994) The cytochrome b5­fold: an adaptable module. Biochimie 76, 674-692.
  11. Mauk, A.G., Mauk, M.R., Moore, G.R. and Northrup, S.H. (1995) Experimental and theoretical analysis of the interaction between cytochrome c and cytochrome b5. J. Bioenerg. Biomembr. 27, 311-330.
  12. Meyer, T.E., Tollin, G. and Cusanovich, M.A. (1994) Protein interaction sites obtained via sequence homology. The site of complexation of electron transfer partners of cytochrome c revealed by mapping amino acid substitutions onto three­dimensional protein surfaces. Biochimie 76, 480-488.
  13. Napier, J.A., Sayanova, O., Stobart, A.K. and Shewry, P.R. (1997) A new class of cytochrome b5 fusion proteins. Biochem. J. 328, 717-718.
  14. Onuchic, J.N., Beratan, D.N., Winkler, J.R. and Gray, H.B. (1992) Pathway analysis of protein electron­transfer reactions. Annu. Rev. Biophys. Biomol. Struct. 21, 349-377.
  15. Roos, P.H. (1996) Chromatographic separation and behavior of microsomal cytochrome P450 and cytochrome b5. J. Chromatogr. B684, 107-131.
  16. Shanklin, J. and Cahoon, E.B. (1998) Desaturation and related modifications of fatty acids. Annu. Rev. Plant Physiol. Plant Mol. Biol. 49, 611-641.
Bibliography on structural studies of cytochromes b5