Abstract
Heme iron in the ferrous state is one of nature’s best di-oxygen sensors.1 A wide variety of protein structural environments incorporate heme and permit either oxygen binding, single electron redox processes, or both. The oxygen transport proteins myoglobin (Mb) and hemoglobin (Hb), for example, alternately bind and release oxygen. The P450 oxygenase2,3 heme proteins and cytochrome c oxidase, also bind oxygen in their biological role and, in addition, shuttle heme in a ferric-ferrous reduction and. reoxidation cycle. The cytochromes, in contrast, do not accept small molecules as a heme axial ligand as both available positions are occupied by amino acid residues from the primary protein structure. The sole function of these proteins is electron transfer by univalent ferric-ferrous redox processes, which are often coupled with energy storage for cellular work. A unique additional property of monoxygenase proteins (as well as the deoxygenases which will not be discussed in this paper) is the sensing of carbon substrates in addition to oxygen.
Supported in part by Grants from the National Institutes of Health AM 00562, GM 21161, GM 18051, and the National Science Foundation BMS 74-01366.
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Footnotes and References
Szent-Gyogyi, A. (1937) “Studies on Biological Oxidation and Some of its Catalysts” Eggenbergersome, Buchhandlung, Budapest.
Gunsalus, I. C., Pederson, T. C. and Sligar, S. G. (1975) Ann. Review Biochem. 44, 377.
Hayaishi, O. (ed.) (1974), “Molecular Mechanisms of Oxygen Activation” Academic Press, New York.
Gunsalus, I. C., Meeks, J. R., Lipscomb, J. D., Debrunner, P. G. and Münck, E. (1974) in “Molecular Mechanisms of Oxygen Activation” (O. Hayaishi, ed.), Academic Press, New York, pp. 559–613.
Mason, H. S. (1957) Adv. Enzymology 19, 79.
Gillett, J. R. et al. (eds.) (1969) “Microsomes and Drug Oxidations”, Academic Press, New York.
Hamberg, M., Samuelsson, B., Bjorkhen, I., and Danielsson, H. (1974) in “Molecular Mechanisms of Oxygen Activation” (O. Hayaishi, ed.), Academic Press, New York.
Dickerson, R. E. and Geis, I. “The Structure and Action of Proteins” (1969) Harper-Row, New York.
Sligar, S. G. and Gunsalus, I. C. (1976) Proc. Nat. Acad. Sci. USA 73, 1078.
Takemori, S., Sato, M., Gomi, T., Suhara, K. and Katagiri, M. (1975) Biochem. Biophys. Res. Comm. 67, 1151.
Guengerich, F. P., Ballou, D. P. and Coon, M. J., J. Biol. Chem. 250, 7405.
Fridovich, J. (1974) in “Molecular Mechanisms of Oxygen Activation” (O. Hayaishi, ed.) Academic Press, New York.
Yu, G. A., Gunsalus, I. C., Katagiri, M., Suhara, K. and Takemori, S. (1974) J. Biol. Chem. 249, 94.
Lovenberg, W., (ed.) (1973) “Iron-Sulfur Proteins”, Vol. I, Academic Press, New York.
Tanaka, M., Haniu, M. and Yasunobu, K. (1973) J. Biol. Chem. 248, 1141.
Tanaka, M., Haniu, M., Yasunobu, K. T., Dus, K. and Gunsalus, I. C. (1974) J. Biol. Chem. 249, 3689.
Sligar, S. G., Debrunner, P. G., Lipscomb, J. D., Namtvedt, M. J. and Gunsalus, I. C. (1974) Proc. Nat. Acad. Sci. USA 71, 3906.
Lipscomb, J. D., Sligar, S. G., Namtvedt, M. J. and Gunsalus, I. C. (1976) J. Biol. Chem. 251, 1116.
Sligar, S. (1975) Ph.D. Thesis, University of Illinois, Urbana.
Sharrock, M., Münck, E., Debrunner, P. G., Marshall, V. P., Lipscomb, J. D., and Gunsalus, I. C. (1973) Biochemistry 12, 258.
Sharrock, M., Debrunner, P. G., Schulz, C., Lipscomb, J. D., Marshall, V. and Gunsalus, I. C. (1976) Biochem. Biophys. Acta 420, 8.
Champion, P. M., Lipscomb, J. D., Münck, E., Debrunner, P. G. and Gunsalus, I. C. (1975) Biochemistry 14, 4151.
Boyd, G. S. and Smellie, R. M. S. (eds.) “Biological Hydroxy-lation Mechanisms”, Biochem. Soc. Symp. 34, Academic Press, New York.
Sligar, S. G., Lipscomb, J. D., Debrunner, P. G. and Gunsalus, I. C. (1974) Biochem. Biophys. Res. Commun. 61, 290.
Rahimtula, A., O’Brien, P., Hrycay, E., Peterson, J. and Estabrook, R. (1974) Biochem. Biophys. Res. Comm. 60, 695.
Coon, M. J. et al. (1976) Adv. Exp. Medicine and Biology, 74, 270.
Hrycay, E., Gustafsson, J., Ingelman-Sundberg, M. and Ernster, L. (1975) Biochem. Biophys. Res. Comm. 66, 209.
Sligar, S. G., Shastry, B. S. and Gunsalus, I. C. (1976) in “Microsomes and Drug Oxidations” (V. Ullrich, ed.) Plenum Press, New York.
Hollenberg, P., and Hager, L. (1973) J. Biol. Chem. 248, 2630.
Dolphin, D., Forman, D., Borg, J., Fajer, J. and Felton, R. (1971) Proc. Nat. Acad. Sci. USA 68, 614.
Austin, R. H., Beeson, K. W., Eisenstein, L., Frauenfelder, H. and Gunsalus, I. C. (1975) Biochemistry 14, 5355.
Austin, R. H., Beeson, K., Eisenstein, L., Frauenfelder, H., Gunsalus, I. C. and Marshall, V. P. (1973) Science 181, 541.
Alberding, N., Austin, R. H., Chan, Shirley S., Eisenstein, L., Frauenfelder, H., Gunsalus, I. C. and Nordlund, T. M. (1976) J. Chem. Phys. 65, 000.
Austin, R. H., Beeson, K. W., Chan, S. S., Debrunner, P. G., Downing, R., Eisenstein, L., Frauenfelder, H. and Nordlund, T. M. (1976) Rev. Sci. Instrum. 47, 445.
Austin, R. H., Beeson, K. W., Eisenstein, L., Frauenfelder, H., Gunsalus, I. C. and Marshall, V. P. (1974) Phys. Rev. Letters 32, 403.
Mieyal, J. J., Ackerman, R. S., Blumen, J. L. and Freeman, L. S. (1976) J. Biol. Chem. 251, 3436.
Pederson, T. C., Austin, R. H. and Gunsalus, I. C. (1976) in “Microsomes and Drug Oxidations” (V. Ullrich, ed.) Plenum Press, New York.
Dayhoff, M. O. (ed.) (1972) “Atlas of Protein Sequence and Structure” Vol. V, The National Biochemical Research Foundation.
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Gunsalus, I.C., Sligar, S.G., Nordlund, T., Frauenfelder, H. (1977). Oxygen Sensing Heme Proteins: Monoxygenases, Myoglobin and Hemoglobin. In: Reivich, M., Coburn, R., Lahiri, S., Chance, B. (eds) Tissue Hypoxia and Ischemia. Advances in Experimental Medicine and Biology, vol 78. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9035-4_3
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