Abstract
CYTOCHROME b5 is a haem-containing protein in the microsomes of liver tissue. It interacts specifically with a flavo-protein, cytochrome b5 reductase, which catalyses the transfer of electrons from NADH to the haem iron of the cytochrome1. The microsomal cytochrome b5 system has been implicated in fatty acid desaturation reactions2, and a similar system in erythrocytes may catalyse the reduction of methaemoglobin3. Calf liver cytochrome b5, solubilized by pancreatic lipase, has a molecular weight of 11,000 and consists of ninety-three amino-acids in the sequence shown in Fig. 1 (refs. 4 and 5). The haem group is non-covalently bound to the protein and can be removed reversibly by acid acetone treatment6.
This is a preview of subscription content, access via your institution
Access options
References
Strittmatter, P., and Velick, S. F., J. Biol. Chem., 228, 785 (1957).
Oshino, N., Imai, Y., and Sato, J., J. Biochem., Tokyo, 69, 155 (1971).
Hultquist, D. E., and Passon, P. G., Nature New Biology, 229, 252 (1971).
Ozols, J., and Strittmatter, P., J. Biol. Chem., 243, 3376 (1968).
Ozols, J., and Strittmatter, P., J. Biol. Chem., 244, 6617 (1969).
Strittmatter, P., and Velick, S. F., J. Biol. Chem., 221, 253 (1956).
Mathews, F. S., and Strittmatter, P., J. Mol. Biol., 41, 295 (1969).
Mathews, F. S., Levine, M., and Argos, P., in Probes of Structure and Function of Macromolecules and Membranes (edit. by Chance, B., Lee, C. P., and Yonetani, T.) (Academic Press, New York, in the press).
Matthews, B. W., Acta. Cryst., 20, 230 (1966).
Stryer, L., Ann. Rev. Biochem., 37, 25 (1968).
Watson, H. E., Progressin Stereochemistry, 4, 255 (Butterworth, London, 1969).
Dickerson, R. E., Takano, T., Eisenberg, D., Kallai, O. B., Samson, L., Cooper, A., and Margoliash, E., J. Biol. Chem., 246, 1511 (1971).
Spatz, L., and Strittmatter, P., Proc. US Nat. Acad. Sci., 68, 1042 (1971).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
MATHEWS, F., LEVINE, M. & ARGOS, P. The Structure of Calf Liver Cytochrome b5 at 2.8 Å Resolution. Nature New Biology 233, 15–16 (1971). https://doi.org/10.1038/newbio233015a0
Received:
Revised:
Issue date:
DOI: https://doi.org/10.1038/newbio233015a0
This article is cited by
-
Cloning of DNA fragments complementary to tobacco nitrate reductase mRNA and encoding epitopes common to the nitrate reductases from higher plants
Molecular and General Genetics MGG (1987)
-
Identification of the haem ligands of cytochrome b562 by X-ray and NMR methods
Nature (1978)
-
Structural patterns in globular proteins
Nature (1976)
-
Synthesis and reaction with hemin of fragment (62–93) of the polypeptide chain of cytochrome b5
Chemistry of Natural Compounds (1972)
