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Part of the book series: The Jerusalem Symposia on Quantum Chemistry and Biochemistry ((JSQC,volume 9-1))

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Abstract

The metalloproteins are widely distributed in living systems, and they function in key cellular processes. The metal complexes which characterize these proteins have been studied by a variety of physical methods, and the complete three-dimensional structures of a number of metalloproteins have been determined by single crystal, X-ray analysis. The electron density maps on which the X-ray models are based seldom reach atomic resolution, however, and important structural features of the complexes may not be clear in the maps. The purpose of this account is to indicate the detail that can be visualized at several resolutions, to summarize the structural information on complexes in metalloproteins that have been studied by single crystal, X-ray methods, and to discuss and compare the complexes in several iron proteins.

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References

  • Adman, E.T., Sieker, L.C., and Jensen, L.H.: 1073, The structure of a Bacterial Ferredoxin, J. Biol. Chem., 248, 3987–3996.

    Google Scholar 

  • Adman, E.T., Watenpaugh, K.D., and Jensen, L.H.: 1975, NH…S Hydrogen Bonds in Peptococcus aerogenes Ferredoxin, Clostridium pasteurianum Rubredoxin, and Chromatium High Potential Iron Protein, Proc. Nat. Acad. Sci. U.S.A. 72, 4854–4858.

    Article  CAS  Google Scholar 

  • Adman, E.T., Sieker, L.C., and Jensen, L.H.: 1976, Structure of P. aerogenes Ferredoxin: Refinement at 2 Ã… Resolution, J. Biol. Chem. 251, 3801–3806.

    CAS  Google Scholar 

  • Arnone, A., Bier, C.J., Cotton, F.A., Day, V.W., Hazen, Jr., E.E., Richardson, D.C., Richardson, J.S., and in part, Yonath, A.: 1971, A High Resolution Study of an Inhibitor Complex of the Extracellular Nuclease of Staphylococus aureus, J. Biol. Chem., 246, 2302–2316.

    CAS  Google Scholar 

  • Ashida, T., Tanaka, N., Yamane, T., Tsukihara, T., and Kakudo, M.: 1973. The Crystal Structure of Bonito (Katsuo) Ferrocytochrome c at 2.3 Ã… Resolution, J. Biol. Chem. 73, 463–465.

    CAS  Google Scholar 

  • Blundel, T.L., Cutfield, J.F., Dodson, E.J., Dodson, G.G., Hodgkin, D.C., and Mercola, D.A.: 1971, The Crystal Structure of Rhombohedral 2 Zinc Insulin, Cold Spring Harbor Symposia on Quantitative Biology, voL XXXVI, pp. 233–241.

    Google Scholar 

  • Bode, W. and Schwager, P.: 1975, The Refined Crystal Structure of Bovine 3-Trypsin at 1.8 Ã… Resolution, J. Molecular Biol. 98., 693–717.

    Article  CAS  Google Scholar 

  • Cammack, R.: 1973, ‘Super-Reduction of Chromatium High Potential Iron-Sulfur Protein in the Presence of Dimethyl Sulfoxide’, Biochem. Biophys. Res. Commun. 54, 548–554.

    Article  CAS  Google Scholar 

  • Carter, Jr., C.W., Kraut, J., Freer, S.T., Alden, R.A., Sieker, L.C., Adman, E., and Jensen, L.H.: 1972, ‘A Comparison of Fe4S4 * Clusters in High-Potential Iron Protein and in Ferredoxin’, Proc. Nat. Acad. Sci. U.S.A. 69, 3526–3529.

    Article  CAS  Google Scholar 

  • Carter, Jr., C.W., Kraut, J., Freer, S.T., Xuong, N., Alden, R.A., and Bartsch, R.G.: 1974a, ‘Two-Ã…ngstrom Crystal Structure of Oxidized Chromatium High Potential Iron Protein’, J. Biol. Chem. 249, 4212–4225.

    CAS  Google Scholar 

  • Carter, Jr., C.W., Kraut, J., Freer, S.T., and Alden, R.A.: 1974b: ‘Comparison of Oxidation-Reduction Site Geometries in Oxidized and Reduced Chromatium High Potential Iron Protein and Oxidized Peptococcus aerogenes Ferredoxin’ 249, 6339–6346.

    CAS  Google Scholar 

  • Coleman, P.M., Jansonius, J.N., and Matthews, B.W.: 1972 ‘The Structure of Thermolysin: An Electron Density Map at 2.3 Ã… Resolution’, J. Molecular Biol. 70, 701–724.

    Article  Google Scholar 

  • Dickerson, R.E., Tanako, T., Eisenberg, D., Kalli, O.B., Samson, L., Cooper, A., and Margoliash, E.: 1971 ‘Ferricytochrome c I’, J. Biol. Chem. 246, 1511–1535.

    CAS  Google Scholar 

  • Edelman, G.M., Cunningham, B.A., Reeke, Jr., G.N., Becker, J.W., Waxdal, M.J., and Wang, J.L.: 1972, ‘The Covalent and Three-Dimensional Structure of Concanavalin A’, Proc. Nat. Acad. Sci., U.S.A. 69, 2580–2584.

    Article  CAS  Google Scholar 

  • Eklund, H., Nordström, B., Zeppezauer, E., Söderland, G., Ohlsson, I., Boiwe, T., Söderberg, B.-O., Tapia, O., and Bränden, C.-I.: 1976, ‘The Three-Dimensional Structure of Horse Liver Alcohol Dehydrogenase at 2.4 A Resolution’, J. Molecular Biol., in press.

    Google Scholar 

  • Fenna, R.E. and Matthews, B.W.: 1975, ‘Chlorophyll Arrangement in a Bacteriochlorophyll Protein from Chlorobium limicola’, Nature 258, 573–577.

    Article  CAS  Google Scholar 

  • Freer, S.T., Alden, R.A., Carter, Jr., C.W., and Kraut, J.: 1975, ‘Crystallographic Structure Refinement of Chromatium High Potential Iron Protein at Two Ã…ngstrom Resolution’, J. Biol. Chem. 250, 46–54.

    CAS  Google Scholar 

  • Hendrickson, W.A., Klippenstein, G.L., and Ward, K.B.: 1975, ‘Tertiary Structure of Myohemerythrin at Low Resolution’, Proc. Nat. Acad. Sci., U.S.A. 72, 2160–2164.

    Article  CAS  Google Scholar 

  • Hendrickson, W.A. and Ward, K.B.: 1975, ‘Atomic Models for the Polypeptide Backbones of Myohemerythrin and Hemerythrin’, Biochem. Biophys. Res. Commun. 66, 1349–1356.

    Article  CAS  Google Scholar 

  • Herriot, J.R., Sieker, L.C., Jensen, L.H., and Lovenberg, W.: 1970, ‘Structure of Rubredoxin: An X-ray Study to 2.5 Ã… Resolution’, J. Molecular Biol. 50, 391–406.

    Article  Google Scholar 

  • Herskovitz, T., Averill, B.A., Holm, R.H., Ibers, J.A., Phillips, W.D., and Weiher, J.F.: 1972, ‘Structure and Properties of a Synthetic Analogue of Bacterial Iron-Sulfur Proteins’, Proc. Nat. Acad. Sci., U.S.A. 69, 2437–2441.

    Article  CAS  Google Scholar 

  • Huber, R., Epp, O., and Formanek, H.: 1969, ‘The Environment of the Haem Group in Erythrocruorin (Chironomus thummi)’, J. Molecular Biol. 42 591–594.

    Article  CAS  Google Scholar 

  • Huber, R., Epp, O., and Formanek, H.: 1970, ‘Structures of Deoxy-and Carbonmonoxy Erythrocruorin’, J. Molecular Biol. 52, 349–354.

    Article  CAS  Google Scholar 

  • James, R.W.: 1948, ‘False Detail in Three-Dimensional Fourier Representations of Crystal Structures’, Acta Crystallographica 1, 132–134.

    Article  CAS  Google Scholar 

  • Jensen, L.H.: 1974, ‘Protein Model Refinement Based on X-ray Data’, Ann. Rev. Biophys. Bioengin. 3, 81–93.

    Article  CAS  Google Scholar 

  • Kendrew, J.C.: 1962, ‘Side-Chain Interactions in Myoglobin’, Brookhaven Symposia in Biology, No. 15, 216–228.

    CAS  Google Scholar 

  • Kendrew, J.C.: 1963, ‘Myoglobin and the Structure of Proteins’, Science 139, 1259–1266.

    Article  CAS  Google Scholar 

  • Klippenstein, G.L., Holleman, J.W., and Klotz, I.M.: 1968, ‘The Primary Structure of Golfingia gouldii Hemerythrin. Order of Peptides in Fragments Produced by Tryptic Digestion of Succinylated Hemerythrin. Complete Amino Acid Sequence’, Biochem. 7, 3868–3878.

    Article  CAS  Google Scholar 

  • Kretsinger, R.H. and Nuckolds, C.E.: 1973, ‘Carp Muscle Calcium-Binding Protein’ J. Biol. Chem. 248, 3313–3326.

    CAS  Google Scholar 

  • Liljas, A., Kannan, K.K., Bergsten, P-C., Waara, I., Friborg, K., Strandberg, B., Carlstrom, U., Jäpur, L., Lövgren, S., and Petef, M.: 1972, ‘The Crystal Structure of Human Carbonic Anhydrase C.’, Nature, New Biology 235, 131–137.

    CAS  Google Scholar 

  • Lipscomb, W.N.: 1971, ‘Structures and Mechanisms of Enzymes’, The Robert A. Welch Foundation Conferences on Chemical Research, vol. XV, pp. 131–182.

    Google Scholar 

  • Mathews, F.S., Argos, P., and Levine, M.: 1971 ‘The Structure of Cyto-chrome b5 at 2.0 A Resolution’, Cold Spring Harbor Symposium on Quantitative Biology, vol. XXXVI, pp. 387–395.

    Google Scholar 

  • Perutz, M.F.: 1969, ‘The Haemoglobin Molecule’, Proc. Roy. Soc., B 173, 113–140.

    Article  CAS  Google Scholar 

  • Pulsinelli, P.D., Perutz, M.F., and Nagel, R.L.: 1973, ‘Structure of Hemoglobin M Boston, a Variant with a Five-Coordinated Ferric Herne’, Proc. Nat. Acad. Sci., U.S.A. 70, 3870–3874.

    Article  CAS  Google Scholar 

  • Richardson, J.S., Thomas, K.A., Rubin, B.H., and Richardson, D.C.: 1975, ‘Crystal Structure of Bovine Cu, Zn Superoxide Dismutase at 3 A Resolution: Chain Tracing and Metal Ligands’, Proc. Nat. Acad. Sci., U.S.A. 72, 1349–1353.

    Article  CAS  Google Scholar 

  • Salemme, F.R., Freer, S.T., Xuong, Ng.H., Alden, R.A., and Kraut, J.: 1973, ‘The Structure of the Oxidized Cytochrome c2 of Rhodospirillum rubrum’, J. Biol. Chem. 248, 3910–3921.

    CAS  Google Scholar 

  • Sieker, L.C., Adman, E., and Jensen, L.H.: 1972, ‘Structure of the Fe-S Complex in a Bacterial Ferredoxin’, Nature 235, 40–42.

    Article  CAS  Google Scholar 

  • Stenkamp, R.E., Sieker, L.C., Jensen, L.H., and Loehr, J.S.: 1976a, ‘Structure of Methemerythrin at 5 Ã… resolution’, J. Molecular Biol. 100, 23–34.

    Article  CAS  Google Scholar 

  • Stenkamp, R.E., Sieker, L.C., and Jensen, L.H.: 1976b, ‘Structure of the Iron Complex in Methemerythrin’, Proc. Nat. Acad. Sci., U.S.A. 73, 349–351.

    Article  CAS  Google Scholar 

  • Ward, K.B., Hendrickson, W.A., and Klippenstein, G.L.: 1975, ‘Quaternary and Tertiary Structure of Hemerythrin’, Nature 257, 818–821.

    Article  CAS  Google Scholar 

  • Watenpaugh, K.D., Sieker, L.C., Herriott, J.R., and Jensen, L.H.: 1971, ‘The Structure of a Non-Heme Iron Protein: Rubredoxin at 1,5 Ã… Resolution’, Cold Spring Harbor Symposia on Quantitative Biology, vol. XXXVI, pp. 359–367.

    Google Scholar 

  • Watenpaugh, K.D., Sieker, L.C., Herriott, J.R., and Jensen, L.H.: 1973, ‘Refinement of the Model of a Protein: Rubredoxin at 1.5 Ã… Resolution’, Acta Crystallographica B29, 943–956.

    Google Scholar 

  • Watson, H.C.: 1969, ‘The Stereochemistry of the Protein Myoglobin’, Progr. Stereochem. 4, 299–333. London, Butterworth.

    CAS  Google Scholar 

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© 1977 D. Reidel Publishing Company

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Jensen, L.H. (1977). Metal Complexes in Proteins. In: Pullman, B., Goldblum, N. (eds) Metal-Ligand Interactions in Organic Chemistry and Biochemistry. The Jerusalem Symposia on Quantum Chemistry and Biochemistry, vol 9-1. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-1170-9_14

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  • DOI: https://doi.org/10.1007/978-94-010-1170-9_14

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-1172-3

  • Online ISBN: 978-94-010-1170-9

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