Summary
Analysis of published data on the cysteine and half-cystine content of proteins indicates that most intracellular proteins may be classified as sulfhydryl proteins (those containing cysteine but little or no half-cystine) and that such sulf-hydryl proteins have a low cysteine content. The mean cysteine content found for 32 intracellular mammalian proteins was 1.6 % and intracellular proteins of many bacteria have similar or lower values. Extracellular mammalian proteins are primarily disulfide proteins (those containing half-cystine but little or no cysteine) and have a high half-cystine content, the mean value found for some 34 extracellular mammalian proteins being 4.1 %. This is contrasted with many of the extracellular proteins from facultative bacteria which are cyst(e)ine-free proteins, being lacking in both cysteine and half-cystine. These and related observations are interpreted in terms of the evolution of life in a reducing atmosphere and the subsequent transition to an oxidizing environment. It is suggested that disulfide proteins evolved primarily after the accumulation of oxygen in the atmosphere.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
References
Banaszak, L.J., Bradshaw, R.A., (1975). The enzymes, P.D. Boyer, ed., 3rd ed., Vol. XI, p. 369. New York: Academic Press
Barron, E.S.G., Singer, T.P. (1943). Science97, 356
Bieber, H., Zimmermann, W., (1971). Zbl. Bakt., I. Abt. Orig.217, 47
Dickerson, R.E., Timkovitch, R. (1975). The enzymes, P.D. Boyer, ed., 3rd ed., Vol. XI, p. 397. New York: Academic Press
Friedman, M. (1973). The chemistry and biochemistry of the sulfhydryl group in amino acids., peptides and proteins. New York: Pergamon Press
Gatlin, L.L. (1974). J. Mol. Evol.3, 189
Gatlin, L.L. (1976). J. Mol. Evol.7, 185
Gertler, A., Trop, M. (1971). Eur. J. Biochem.19, 90
Harper, E., Seifter, S. (1974). Isr. J. Chem.12, 515
Harris, J. I., Waters, M. (1976). The enzymes, P.D. Boyer, ed., 3rd ed., Vol. XIII, p. 1. New York: Academic Press
Haugaard, N. (1968). Physiol. Rev.48, 311
Holmquist, R. (1975). J. Mol. Evol.4, 277
Jocelyn, P.C. (1972). Biochemistry of the SH Group, Chapt. 1. New York: Academic Press
Jukes, T.H., Holmquist, R., and Moise, H. (1975). Science,189, 50
Kimura, M. (1968). Genet. Res., Camb.11, 247
King, J.L., Jukes, T.H. (1969). Science164, 788
Liu, T.Y., Elliott, S.D. (1971). The enzymes, P.D. Boyer, ed., Vol. III, p. 609. New York: Academic Press
Malkin, R. (1973). Iron-Sulfur Proteins, W. Lovenberg, ed., Vol. II, p. 1. New York: Academic Press
Markland, Jr., F.S., Smith, E.L. (1971). The enzymes, P.D. Boyer, ed., 3rd ed., Vol. III p. 561. New York: Academic Press
Matsubara, H., Feder, J. (1971). The enzymes, P.D. Boyer, ed., 3rd ed., Vol. III, p. 721. New York: Academic Press
Miller, T.E., Stone, R.W. (1938). J. Bacteriol.36, 248
Mitchell, W.M., Harrington, W.F. (1968). J. Biol. Chem.243, 4683
Murphey, W.H., Barnaby, C., Lin, F.J. and Kaplan, N.O. (1967). J. Biol. Chem.242, 1548
Ohta, T., Kimura, M. (1971). Science174, 150
Olafson, R.W., Jurasek, L., Carpenter, M.R., and Smillie, L.B. (1975). Biochemistry14, 1168
Olson, M.O.J., Nagabhushan, N., Dzwinill, M., Smillie, L.B., and Whitaker, D.R. (1970). Nature228, 438
Pollock, M.R., (1962). The bacteria, I.C. Gunsalas, R.Y. Stanier, eds., Vol. IV, p. 121. New York: Academic Press
Pollock, M.R., Richmond, M.H. (1962). Nature194, 446
Reddy, M.N., Keim, P.S., Heinrikson, R.L., Kezdy, R.J. (1975). J. Biol. Chem.250, 1741
Reeck, G.R., (1970). Handbook of biochemistry, H.A. Sober, ed., 2nd ed., p. C282. Cleveland: Chemical Rubber Company
Reeck, G.R., Fisher, L. (1973). Int. J. Peptide Res.5, 109
Rosenberg, S.A., Guidotti, G. (1968). J. Biol. Chem.243, 1985
Saheb, S.A. (1976). Biochimie58, 793
Smith, M.H. (1966). J. Theoret. Biol.13, 261
Williams, Jr., C.H. (1976). The enzymes, P.D. Boyer, ed., 3rd ed., Vol. XIII, p. 90. New York: Academic Press