Abstract
From the preceding chapters it is clear that a high-resolution crystal structure of P-450 is very desirable and that the obvious candidate for crystallographic studies is P-450cam. Indeed, some of the earliest studies on P-450cam resulted in its crystallization by Yu et al. in 1974.1 However, these crystals, designated orthorhombic I,2 were unsuitable for X-ray diffraction studies and it was not until 1982 that the first X-ray-quality crystals were reported.2 Gunsalus’s group and especially the efforts of G. C. Wagner were instrumental in reaching this milestone.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Yu, C.-A., Gunsalus, I. C., Katagiri, M., Suhara, K., and Takemori, S., 1974, Cytochrome P-450cam: Crystallization and properties, J. Biol. Chem. 249: 94 - 101.
Poulos, T. L., Perez, M., and Wagner, G. C., 1982, Preliminary crystallographic studies on cytochrome P-450cam, J. Biol. Chem. 257: 10427 - 10429.
Lipscomb, J. D., Harrison, J. E., Dus, K. M., and Gunsalus, I. C., 1978, Cytochrome P-450cam: Ss-dimer and -SH derivative reactivities, Biochem. Biophys. Res. Commun. 83: 771 - 778.
Finzel, B., 1983, Crystallographic refinement of cytochrome c peroxidase at 1. 7 A resolution, Ph.D. thesis, University of California, San Diego.
Haniu, M., Armes, L. G., Yasunobu, K. T., Shastry, B. A., and Gunsalus, I. C., 1982, Amino acid sequence of the Pseudomonas putida cytochrome P450, J Biol. Chem. 257: 12664 - 12671.
Hendrickson, W. A., and Konnert, J. H., 1980, Stereochemically restrained crystallographic least-squares refinement of macromolecular structures, In: Computing in Crystallography (R. Diamond, S. Ramseshan, and K. Venkatesan, eds.), Indian Institute of Science, Bangalore, pp. 1301 - 1323.
Devaney, P., Wagner, G. C., Debrunner, P. G., and Gunsalus, I. C., 1980, Single crystal ESR of cytochrone P-450,, from Pseudomonas putida, Fed. Pt-oc. 39: 11 - 39.
Gunsalus, I. C., Wagner, G. C., and Debrunner, P. G., 1980, Probes of cytochrome P450 structure, In: Microsomes, Drug Oxidation and Chemical Carcinogenesis ( M. J. Coon, A. H. Conney, R. W. Estabrook, H. V. Gelboin, J. R. Gillette, and P. J. O’Brien, eds.), Academic Press, New York, pp. 233 - 242.
Richardson, J., 1981, The anatomy and taxonomy of protein structure, Adv. Protein Chem. 34: 167 - 339.
Ortiz de Montellano, P. R., Kunze, K. L., and Beilan, H. S., 1983, Chiral orientation of prosthetic heme in the cytochrome P450 active site, J. Biol. Chem. 258: 45 - 47.
Perutz, M. F., Muirhead, H., Cox, J. M., and Guaman, L. G., 1968, Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: The atomic model, Nature 219: 131 - 139.
Murthy, M. R. N., Reid, T. J., Sicignano, A., Tanaka, N., and Rossmann, M. G., 1981, Structure of beef liver catalase, J. Mol. Biol. 152: 465 - 499.
Poulos, T. L., Freer, S. T., Alden, R. A., Xuong, N. H., Edwards, S. L., Hamlin, R. C., and Kraut, J., 1978, Crystallographic determination of the heme orientation and location of the cyanide binding site in cytochrome c peroxidase, J. Biol. Chem. 257: 10427 - 10429.
Salemme, F. R., 1977, Structure and function of cytochrome c, Annu. Rev. Biochem. 46: 299 - 329.
Poulos, T. L., and Finzel, B. C., 1984, Herne enzyme structure and function, In:Peptide and Protein Reviews, Volume 4 ( M. T. W. Hearn, ed.), Dekker, New York, pp. 115 - 171.
Asakura, T., and Yonetani, T., 1969, Studies on cytochrome c peroxidase: Recombination of apoenzyme with protoheme dialkyl esters and etioheme, J. Biol. Chem. 244: 4573 - 4579.
Bosshard, H. R., Banziger, J., Hasler, T., and Poulos, T. L., 1984, The ctyochrome c peroxidase-cytochrome c electron transfer complex: The role of histidine residues, J. Biol. Chem. 259: 5683 - 5690.
Champion, P. M., Gunsalus, I. C., and Wagner, G. C., 1978, Resonance Raman investigations of cytochrome P-450cam from Pseudomonas putida, J. Am. Chem. Soc. 100: 3743 - 3751.
Champion, P. M., Stallard, B. R., Wagner, G. C., and Gunsalus, I. C., 1982, Resonance Raman detection of an Fe—S bond in cytochrome P-450cam, J. Am. Chem. Soc. 104: 54695472.
Valentine, J. S., Sheridan, R. P., Allen, L. C., and Kahn, P. L., 1979, Coupling between oxidation state and hydrogen bond conformation in heure proteins, Proc. Natl. Acad. Sci. USA 76: 1009 - 1013.
Dawson, J. H., Andersson, L. A., and Sono, M., 1982, Spectroscopic investigations of cytochrome P-450cam-ligand complexes: Identification of the ligand trans to cysteinate in the native enzyme, J. Biol. Chem. 257: 3606 - 3617.
Kunze, K. L., Mangold, B. L. K., Wheeler, C., Beilan, H. S., and Ortiz de Montellano, P. R., 1983, The cytochrome P450 active site: Regiospecificity of prosthetic heme alkylation by olefins and acetylenes, J. Biol, Chem. 258: 4202 - 4207.
Fujii-Kuriyama, Y., Mizumaki, Y., Kawajiri, K., Sugawa, K., and Muramatsu, M. C., 1982, Primary structure of a cytochrome P450: Coding nucleotide sequence of phenobarbital inducible cytochrome P450 cDNA from rat liver, Proc. Natl. Acad. Sci. USA 79: 2793 - 2797.
Heinemann, F. S., and Ozols, J., 1982, The covalent structure of rabbit phenobarbital-induced cytochrome P450: Partial amino acid sequence and order of cyanogen bromide peptides, J. Biol. Chem. 257: 14988 - 14999.
Black, S. D., Tarr, G. E., and Coon, M. J., 1982, Structural features of isozyme 2 of liver microsomal cytochrome P450, J. Biol. Chem. 257: 14616 - 14619.
Tarr, G. E., Black, S. D., Fujita, V. S., and Coon, M. J., 1983, Complete amino acid sequence and predicted membrane topology of phenobarbital induced cytochrome P450 (isozyme 2) from rabbit liver microsomes, Proc. Natl. Acad. Sci. USA 80: 65521 - 6556.
Morohashi, K., Fujii-Kuriyama, Y., Okada, Y., Sogawa, K., Hirose, T., and Inayama, S., 1984, Molecular cloning and nucleotide sequence of cDNA for mRNA of mito- chondrial cytochrome P450 (SCC) of bovine adrenal cortex, Proc. Natl. Acad. Sci. USA 81: 4647 - 4651.
Volz, K. W., Matthews, D. A., Alden, L. A., Freer, S. T., Hansch, C., Kaufman, B. T., and Kraut, J., 1982, Crystal structure of avian dihydrofolate reductase containing phenyltriazine and NADPH, J. Biol. Chem. 257: 2528 - 2536.
Buehner, M., Ford, G. C., Olsen, K. W., and Rossmann, M. G., 1974, Three dimensional structure of D-glyceraldehyde-3-phosphate dehydrogenase, J. Mol. Biol. 90: 25 - 49.
Blesecker, G., Harris, J. I., Theiry, J. C., Walker, J. E., and Wonacott, A. J., 1977, Sequence and structure of D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus, Nature 266: 328 - 333.
Eventoff, W., Rossmann, M. G., Taylor, S. S., Torf, H. J., Meyer, H., Keil, W., and Kiltz, H. H., 1977, Structural adaptions of lactate dehydrogenase isozymes, Proc. Natl. Acad. Sci. USA 74: 2677 - 2681.
Rossman, M. G., 1983, Structure—function relationships of NAD-dependent dehydrogenases, In: Biological Oxidations ( H. Sund and V. Ullrich, eds.) Springer-Verlag, Berlin, pp. 34 - 54.
Poulos, T. L., and Kraut, J., 1980, The stereochemistry of peroxidase catalysis, J. Biol. Chem. 255: 8199 - 8205.
Jones, P., and Suggett, A., 1968, The catalase—hydrogen peroxide system, Biochem. J. 110: 621 - 629.
Poulos, T. L., 1982, The peroxidase mechanism and the structure of cytochrome c peroxidase, In: Molecular Structure and Biological Activity ( J. E. Griffin and W. L. Duax, eds.), Elsevier, Amsterdam, pp. 79 - 90.
Ariaso, T., Miyoshi, K., and Yamazaki, I., 1976, Mechanisms of electron transfer from sulfite to horseradish peroxidase-hydroperoxide compounds, Biochemistry 15: 3059 - 3063.
Dolphin, D., Forman, A., Borg, D. C., Fajer, J., and Felton, R. H., 1971, Compounds I of catalase and horse radish peroxidase: -rr-Cation radicals, Proc. Natl. Acad. Sci. USA 68: 614 - 618.
Aasa, R., Vanngard, T., and Dunford, H. B., 1975, EPR studies of compound I of horseradish peroxidase, Biochim. Biophys. Acta 391: 259 - 264.
King, N. K., and Winfield, M. E., 1963, The mechanisms of myoglobin oxidation, J. Biol. Chem. 238: 1520 - 1528.
White, R. E., Sligar, S. G., and Coon, M. J., 1980, Evidence for a homolytic mechanism of peroxide oxygen-oxygen bond cleavage during substrate hydroxylation by cytochrome P450, J. Biol. Chem. 255: 1108 - 1111.
White, R. E., and Coon, M. J., 1980, Oxygen activation by cytochrome P450, Annu. Rev. Biochem. 49: 315 - 356.
McCarthy, M. B., and White, R. E., 1983, Functional differences between compound I and the cytochrome P450 reactive oxygen intermediate, J. Biol. Chem. 258: 9153 - 9158.
Hamilton, G., 1974, Chemical models and mechanisms for oxygenases, In: Molecular Mechanisms of Oxygen Activation ( O. Hayashi ed.), Academic Press, New York, pp. 405 - 451.
Sligar, S. G., Shastry, B. S., and Gunsalus, I. C., 1977, Oxygen reactions of the P450 heure protein, In: Microsomes and Drug Oxidation ( V. Ullrich, I. Routs, A. Hildebrandt, R. W. Estabrook, and A. H. Cooney, eds.), Pergamon Press, Elmsford, N.Y., pp. 202 - 209.
Gleb, M. H., Heimbrook, D. C., Malkonen, P., and Sligar, S. G., 1982, Stereochemistry and deuterium isotope effects in camphor hydroxylation by the cytochrome P-450cam monoxygenase system, Biochemistry 21: 370 - 377.
Phillips, S. E., 1980, Structure and refinement of oxymyoglobin at 1.6 A resolution, J. Mol. Biol. 142: 531 - 554.
Jameson, G. B., Molinaro, F. S., Ibers, J. A., Coltman, J. P., Brauman, J. I., Rose, E., and Suslick, K. S., 1978, Structural changes upon oxygenation of an iron (II) (porphyrinato) (imidazole) complex, J. Am. Chem. Soc. 100: 6769 - 6770.
Jameson, G. B., Rodley, G. A., Robinson, W. T., Gagne, R. R., Reed, C. A., and Collman, J. R., 1978, Structure of a dioxygen adduct of (1-methylimidazole)-mesotetrakis (a,a,a,a-o-pivalamidophenyl) porphinatoiron (II): An iron dioxygen model for the heme component of oxymyoglobin, lnorg. Chem. 17: 850 - 857.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1986 Springer Science+Business Media New York
About this chapter
Cite this chapter
Poulos, T.L. (1986). The Crystal Structure of Cytochrome P-450cam . In: de Montellano, P.R.O. (eds) Cytochrome P-450. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9939-2_13
Download citation
DOI: https://doi.org/10.1007/978-1-4757-9939-2_13
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4757-9941-5
Online ISBN: 978-1-4757-9939-2
eBook Packages: Springer Book Archive