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Active sites in copper proteins an electronic structure overview

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Copper, Molybdenum, and Vanadium in Biological Systems

Part of the book series: Structure and Bonding ((STRUCTURE,volume 53))

Abstract

A detailed picture of the unique electronic structure of active sites in copper proteins is essential to our understanding of their biological functions. This has been achieved through a combination of complementary spectroscopic techniques, chemical perturbations, and parallel studies on copper complexes which serve as spectral analogues. These studies provide a basis for the generation of a “spectroscopically effective” picture of the active site and allow a correlation of changes in geometric and electronic structure with variation in function. When combined with high-resolution crystallographic information, single crystal spectral studies allow a correlation of electronic features with specific geometric features and provide a great deal of insight into the bonding at the site.

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Abbreviations

CD:

Circular dichroism

cm−1 :

Wavenumber

CT:

Charge transfer

Cys:

Cysteine

ENDOR:

Electron nuclear double resonance

EPR:

Electron paramagnetic resonance

ESCA:

Electron spectroscopy for chemical analysis

eV:

Electron volt

EXAFS:

Extended x-ray absorption fine structure

GHz:

Gigahertz

His:

Histidine

IR:

Infrared

IT:

Intervalent transfer

LEFE:

Linear electric field effect

MCD:

Magnetic circular dichroism

Met:

Methionine

NMR:

Nuclear magnetic resonance

SCF-Xα-SW:

Self-consistent field Xα scattered wave

SOD:

Superoxide dismutase

SQUID:

Superconducting quantum interference detector

T2D:

Type 2 depleted laccase

TT2D:

Treated type 2 depleted laccase

UV:

Ultraviolet

VIS:

Visible

VII. References

  1. Gray, H. B., Solomon, E. I.: Electronic structure of blue copper centers in proteins, in: Copper Proteins (ed.) Spiro, T. G., chapter 1, New York, Wiley-Interscience 1981

    Google Scholar 

  2. Solomon, E. I.: The binuclear copper active site: hemocyanin, tyrosinase and type 3 copper oxidases, ibid.in:, ibid. chapter 2

    Google Scholar 

  3. Ballhausen, C. J.: Introduction to Ligand Field Theory, New York, McGraw-Hill 1962

    Google Scholar 

  4. Mulliken, R. S., Rieke, C. A.: Repts. Progr. Phys. 8, 231 (1941)

    Article  CAS  Google Scholar 

  5. Abragam, A., Bleaney, B.: Electron Paramagnetic Resonance of Transition Ions, Oxford, Clarendon 1970

    Google Scholar 

  6. Maki, A., McGarvey, B.: J. Chem. Phys. 29, 31 (1958)

    Article  CAS  Google Scholar 

  7. Peisach, J., Blumberg, W. E.: Arch. Biochem. Biophys. 165, 691 (1974)

    Article  CAS  Google Scholar 

  8. Walker, F. A., Sigel, H., McCormick, D. B.: Inorg. Chem. 11, 2756 (1972)

    Article  CAS  Google Scholar 

  9. Falk, K.-E. et al.: Inorg. Chem. 3, 556 (1970)

    Article  Google Scholar 

  10. Lewis, W. B., Alei, M., Morgan, L. O.: J. Chem. Phys. 45, 4003 (1966)

    Article  CAS  Google Scholar 

  11. Malmström, B. G., Vänngård, T.: J. Mol. Biol. 2, 118 (1960)

    Google Scholar 

  12. Davis, P. H., White, L. K., Belford, R. L.: Inorg. Chem. 14, 1753 (1975). See discussion in caption of Fig. 5.

    Article  CAS  Google Scholar 

  13. Chow, C., Chang, K., Willett, R. D.: J. Chem. Phys. 59, 2629 (1973)

    Article  CAS  Google Scholar 

  14. Froncisz, W. et al.: J. Biol. Chem. 254, 7482 (1979)

    CAS  Google Scholar 

  15. Feher, G. et al.: Ann. N.Y. Acad. Sci. 222, 86 (1973)

    Article  CAS  Google Scholar 

  16. Mims, W. B., Peisach, J.: Pulsed EPR studies of metalloproteins, in: Biological Applications of Magnetic Resonance (ed.) Schulman, R. G., p. 221, New York, Academic, 1979

    Google Scholar 

  17. Mims, W. B.: The Linear Electric Field Effect in Paramagnetic Resonance, Oxford, Clarendon 1976

    Google Scholar 

  18. Peisach, J., Mims, W. B.: Chem. Phys. Lett. 37, 307 (1976)

    Article  CAS  Google Scholar 

  19. Hathaway, B. J., Billing, D. E.: Coord. Chem. Rev. 5, 143 (1970)

    Article  CAS  Google Scholar 

  20. Holmes, O. G., McClure, D. S.: J. Chem. Phys. 26, 1686 (1957)

    Article  CAS  Google Scholar 

  21. Hathaway, B. J., Stephens, F.: J. Chem. Soc. A, 884 (1970)

    Google Scholar 

  22. McFadden, D. L. et al.: J. Chem. Soc. Dalton Trans. 47 (1976)

    Google Scholar 

  23. McFaden, D. L. et al.: J. Chem. Soc. Dalton Trans. 263 (1975)

    Google Scholar 

  24. McLellan, A. W., Melson, G. A.: J. Chem. Soc. A, 137 (1967)

    Google Scholar 

  25. Ferris, N. S. et al.: J. Am. Chem. Soc. 100, 5939 (1978)

    Article  CAS  Google Scholar 

  26. Glick, M. D. et al.: Inorg. Chem. 15, 1190 (1976)

    Article  CAS  Google Scholar 

  27. Miskowski, V. M. et al.: J. Am. Chem. Soc. 98, 8344 (1976)

    Article  CAS  Google Scholar 

  28. Ou, C. C. et al.: Inorg. Chem. 15, 3157 (1976)

    Article  CAS  Google Scholar 

  29. Hitchman, M. A., Cassidy, P. J.: Inorg. Chem. 18, 1745 (1979)

    Article  CAS  Google Scholar 

  30. Oelkrug, D.: Struct. Bonding 9, 1 (1971)

    CAS  Google Scholar 

  31. Oelkrug, D.: Z. Physik. Chem. N.F. 56, 325 (1967)

    CAS  Google Scholar 

  32. Kato, H.: Mol. Phys. 24, 81 (1972)

    Article  CAS  Google Scholar 

  33. Yasui, T., Hidaka, J., Shimura, Y.: J. Am. Chem. Soc. 87, 2762 (1965)

    Article  CAS  Google Scholar 

  34. Amundsen, A. R., Whelan, J., Bosnich, B.: J. Am. Chem. Soc. 99, 6730 (1977)

    Article  CAS  Google Scholar 

  35. Elliot, H., Hathaway, B. J.: Inorg. Chem. 5, 885 (1966)

    Article  Google Scholar 

  36. Kennedy, B. P., Lever, A. B. P.: J. Am. Chem. Soc. 95, 6907 (1973)

    Article  CAS  Google Scholar 

  37. Bernarducci, E. et al.: J. Am. Chem. Soc. 103, 1686 (1981)

    Article  CAS  Google Scholar 

  38. Fawcett, T. G. et al.: J. Am. Chem. Soc. 102, 2598 (1980)

    Article  CAS  Google Scholar 

  39. Downes, J. M., Whelan, J., Bosnich, B.: Inorg. Chem. 20, 1081 (1981)

    Article  CAS  Google Scholar 

  40. Hughey, J. L. IV et al.: J. Am. Chem. Soc. 101, 2617 (1979)

    Article  CAS  Google Scholar 

  41. Agnus, Y., Louis, R., Weiss, R.: J. Am. Chem. Soc. 101, 3381 (1979)

    Article  CAS  Google Scholar 

  42. Ballhausen, C. J.: The measurement and interpretation of transition ion crystal spectra, in: Spectroscopy in Inorganic Chemistry, Vol. 1 (eds.) Rao, C. N. R., Ferraro, J. R., chapter 1, New York, Academic 1970

    Google Scholar 

  43. Gillard, R. D.: Optical rotatory dispersion and circular dichroism, in: Physical Methods in Advanced Inorganic Chemistry (eds.) Hill, H. A. O., Day, P., chapter 5, New York, Wiley-Interscience 1968

    Google Scholar 

  44. Richardson, F. S.: Chem. Rev. 79, 17 (1979)

    Article  CAS  Google Scholar 

  45. Kuhn, W.: Ann. Rev. Phys. Chem. 9, 417 (1958)

    Article  CAS  Google Scholar 

  46. Stephens, P. J.: Adv. Chem. Phys. 35, 197 (1976)

    Article  CAS  Google Scholar 

  47. Stephens, P. J.: Ann. Rev. Phys. Chem. 25, 201 (1974)

    Article  CAS  Google Scholar 

  48. Eickman, N. C. et al.: J. Am. Chem. Soc. 100, 6529 (1978)

    Article  CAS  Google Scholar 

  49. Freedman, T. B., Loehr, J. S., Loehr, T. M.: J. Am. Chem. Soc. 98, 2809 (1976)

    Article  CAS  Google Scholar 

  50. Larrabee, J. A. et al.: J. Am. Chem. Soc. 99, 1979 (1977)

    Article  CAS  Google Scholar 

  51. Valentine, J. S., Pantoliano, M. W.: Protein-metal ion interactions in cuprozinc protein (superoxide dismutase), in: Copper Proteins (ed.) Spiro, T. G., chapter 8, New York, Wiley-Interscience 1981

    Google Scholar 

  52. Ettinger, M. J., Kosman, D. J.: Chemical and catalytic properties of galactose oxidase, ibid.in:, ibid. chapter 6

    Google Scholar 

  53. Villafranca, J. J.: Dopamine-β-hydroxylase, ibid.in:, ibid. chapter 7

    Google Scholar 

  54. Hamilton, G. A.: Oxidases with monocopper reactive sites, ibid.in:, ibid. chapter 5

    Google Scholar 

  55. Richardson, J. S. et al.: Proc. Nat. Acad. Sci. USA 72, 1349 (1975)

    Article  CAS  Google Scholar 

  56. Weser, U. et al.: Biochim. Biophys. Acta 243, 203 (1971)

    CAS  Google Scholar 

  57. Rotilio, G. et al.: Biochemistry 11, 2187 (1972)

    Article  CAS  Google Scholar 

  58. Lieberman, R. A., Sands, R. H., Fee, J. A.: J. Biol. Chem. 257, 336 (1982)

    CAS  Google Scholar 

  59. Tainer, J. A. et al.: in 250 D: Cu,Zn-Superoxide Dismutase Complete Atomic Coordinates (eds.) Richardson, D. C. and Richardson, J. S., Brookhaven Protein Structure Data Bank 1980

    Google Scholar 

  60. Rotilio, G., Calabrese, L., Coleman, J. E.: J. Biol. Chem. 248, 3855 (1973)

    CAS  Google Scholar 

  61. Weser, U.: Struct. Bonding (Berlin) 17, 1 (1973)

    Article  CAS  Google Scholar 

  62. Fee, J. E., Gaber, B. P.: J. Biol. Chem. 247, 60 (1972)

    CAS  Google Scholar 

  63. Rotilio, G., Rigo, A., Calabrese, L.: Recent developments on the active-site structure and mechanism of bovine copper-and zinc-containing superoxide dismutase, in: Frontiers in Physiochemical Biology (ed.) Pullman, B., chapter 15, New York, Academic 1978

    Google Scholar 

  64. Fee, J. A., Peisach, J., Mims, W. B.: J. Biol. Chem. 256, 1910 (1981)

    CAS  Google Scholar 

  65. Malkin, R., Malmström, B. G.: The state and function of copper in biological systems, in: Advances in Enzymology and Related Areas of Molecular Biology, 33 (ed.) Nord, F. F., p. 177, New York, Interscience 1970

    Chapter  Google Scholar 

  66. Fee, J. A.: Struct. Bonding (Berlin) 23, 1 (1975)

    CAS  Google Scholar 

  67. Solomon, E. I., Hare, J. W., Gray, H. B.: Proc. Nat. Acad. Sci. USA 73, 1389 (1976)

    Article  CAS  Google Scholar 

  68. Solomon, E. I. et al.: J. Am. Chem. Soc., 102, 168 (1980)

    Article  CAS  Google Scholar 

  69. Osborne, G. H., Cheng, J. C., Stephens, P. J.: Rev. Sci. Instrum. 44, 10 (1973)

    Article  CAS  Google Scholar 

  70. Bates, C. A. et al.: Proc. Phys. Soc. 79, 73 (1962)

    Article  CAS  Google Scholar 

  71. Parker, I. H.: J. Phys. C.: Solid St. Phys. 4, 2967 (1971)

    Article  CAS  Google Scholar 

  72. Krishnan, V. G.: J. Chem. Phys. 68, 660 (1978)

    Article  CAS  Google Scholar 

  73. Bates, C. A.: Proc. Phys. Soc. 83, 465 (1964)

    Article  CAS  Google Scholar 

  74. Dietz, R. E. et al.: Phys. Rev. 132, 1559 (1963)

    Article  CAS  Google Scholar 

  75. Roberts, J. E. et al.: J. Am. Chem. Soc. 102, 825 (1980)

    Article  CAS  Google Scholar 

  76. Katoh, S., Takamiya, S.: J. Biochem. (Tokyo) 55, 378 (1964)

    CAS  Google Scholar 

  77. Solomon, E. I. et al.: J. Am. Chem. Soc. 97, 3878 (1975)

    Article  CAS  Google Scholar 

  78. McMillan, D. R., Holwerda, R. A., Gray, H. B.: Proc. Nat. Acad. Sci. USA 71, 1339 (1974)

    Article  Google Scholar 

  79. McMillan, D. R., Rosenberg, R. C., Gray, H. B.: Proc. Nat. Acad. Sci. USA 71, 4760 (1974)

    Article  Google Scholar 

  80. Solomon, E. I. et al.: J. Am. Chem. Soc. 98, 8046 (1976)

    Article  CAS  Google Scholar 

  81. Colman, P. J. et al.: Nature (London) 272, 319 (1978)

    Article  CAS  Google Scholar 

  82. Markley, J. L.: Biochemistry 14, 4428 (1975)

    Article  CAS  Google Scholar 

  83. Penfield, K. W. et al.: J. Am. Chem. Soc. 103, 4382 (1981)

    Article  CAS  Google Scholar 

  84. Desjardins, S. R. et al.: to be published

    Google Scholar 

  85. Tennent, D. L., McMillan, D. R.: J. Am. Chem. Soc. 101, 2307 (1979)

    Article  CAS  Google Scholar 

  86. McMillan, D. R., Morris, M. C.: Proc. Nat. Acad. Sci. USA 78, 6567 (1981)

    Article  Google Scholar 

  87. Peisach, J., Levine, W. G., Blumberg, W. E.: J. Biol. Chem. 242, 2847 (1967)

    CAS  Google Scholar 

  88. Companion, A. L., Komarynsky, M. A.: J. Chem. Educ. 41, 257 (1964)

    Article  CAS  Google Scholar 

  89. Peisach, J., Mims, W. B.: Eur. J. Biochem. 84, 207 (1978)

    Article  CAS  Google Scholar 

  90. Bannister, J. V. (ed.): Structure and Function of Haemocyanin, Berlin, Springer-Verlag 1977

    Google Scholar 

  91. Ghiretti, F.: Arch. Biochem. Biophys. 63, 165 (1956)

    Article  CAS  Google Scholar 

  92. Himmelwright, R. S. et al.: J. Am. Chem. Soc. 102, 5378 (1980)

    Article  CAS  Google Scholar 

  93. Himmelwright, R. S. et al.: J. Am. Chem. Soc. 102, 7339 (1980)

    Article  CAS  Google Scholar 

  94. van Schaick, E. J. M. et al.: The crystal structure of hemocyanin hexamer from Panulirus interruptus at 0.5 nm resolution, in: Invertebrate Oxygen-Binding Proteins (eds.) Lamy, J. and Lamy, J., p. 353, New York, Marcel Dekker 1981

    Google Scholar 

  95. Magnus, K. A., Love, W. E.: Crystals of a 70,000 dalton subunit of Limulus polyphemus hemocyanin, ibid., p. 363

    Google Scholar 

  96. Solomon, E. I. et al.: J. Am. Chem. Soc. 98, 1029 (1976)

    Article  CAS  Google Scholar 

  97. Dooley, D. et al.: Proc. Nat. Acad. Sci. USA 75, 3019 (1978)

    Article  CAS  Google Scholar 

  98. Schugar, H. et al.: J. Am. Chem. Soc. 97, 6442 (1975)

    Article  CAS  Google Scholar 

  99. Hansen, A. E., Ballhausen, C. J.: Trans. Faraday Soc. 61, 631 (1965)

    Article  CAS  Google Scholar 

  100. Smith, T. D., Pilbrow, J. R.: Coord. Chem. Rev. 13, 173 (1974)

    Article  CAS  Google Scholar 

  101. Himmelwright, R. S., Eickman, N. C., Solomon, E. I.: Biochem. Biophys. Res. Comm. 81, 237 (1978)

    Article  CAS  Google Scholar 

  102. Himmelwright, R. S., Eickman, N. C., Solomon, E. I.: Biochem. Biophys. Res. Comm. 81, 243 (1978)

    Article  CAS  Google Scholar 

  103. Himmelwright, R. S., Eickman, N. C., Solomon, E. I.: Biochem. Biophys. Res. Comm. 84, 300 (1978)

    Article  CAS  Google Scholar 

  104. Himmelwright, R. S., Eickman, N. C., Solomon, E. I.: J. Am. Chem. Soc. 101, 1576 (1979)

    Article  CAS  Google Scholar 

  105. Himmelwright, R. S., Eickman, N. C., Solomon, E. I.: Biochem. Biophys. Res. Comm. 86, 628 (1979)

    Article  CAS  Google Scholar 

  106. Eickman, N. C., Himmelwright, R. S., Solomon, E. I.: Proc. Nat. Acad. Sci. USA 76, 2094 (1979)

    Article  CAS  Google Scholar 

  107. Robin, M. B., Day, P.: Adv. Inorg. Chem. and Radiochem. 10, 247 (1967)

    CAS  Google Scholar 

  108. Wilcox, D. E., Mims, W. B., Solomon, E. I.: to be published

    Google Scholar 

  109. Fenton, D. E., Schroeder, R. R., Lintvedt, R. L.: J. Am. Chem. Soc. 100, 1931 (1978)

    Article  CAS  Google Scholar 

  110. Gagné, R. R. et al.: J. Am. Chem. Soc. 101, 4571 (1979)

    Article  Google Scholar 

  111. Gatteschi, D., Mealli, C., Sacconi, L.: Inorg. Chem. 15, 2774 (1976)

    Article  CAS  Google Scholar 

  112. Gagné, R. R., Henling, L. M., Kistenmacher, T. J.: Inorg. Chem. 19, 1226 (1980)

    Article  Google Scholar 

  113. van der Deen, H., Hoving, H.: Biochemistry 16, 3519 (1977)

    Article  Google Scholar 

  114. Schoot Uiterkamp, A. J. M.: FEBS Lett, 20, 93 (1972)

    Article  CAS  Google Scholar 

  115. Schoot Uiterkamp, A. J. M., Mason, H. S.: Proc. Nat. Acad. Sci. USA 70, 993 (1973)

    Article  CAS  Google Scholar 

  116. Schoot Uiterkamp, A. J. M. et al.: Biochim. Biophys. Acta 372, 407 (1974)

    CAS  Google Scholar 

  117. These simulation programs, based on a perturbation approach, have been used to estimate the metal-metal distance for a number of dipolar-coupled (|2J|<30 cm−1) cupric complexes (Boyd, P. D. W. et al.: J. Chem. Soc. Dalton, 1549 (1973)) and show good agreement when compared with x-ray crystallographic results

    Google Scholar 

  118. Witters, R., Lontie, R.: FEBS Lett. 60, 400 (1965)

    Article  Google Scholar 

  119. Felsenfeld, G., Printz, M. P.: J. Am. Chem. Soc. 81, 6259 (1959)

    Article  CAS  Google Scholar 

  120. Witters, R., DeLey, M., Lontie, R.: The reaction of Helix pomatia methemocyanin with azide and fluoride, in: Structure and Function of Haemocyanin (ed.) Bannister, J. V., p. 239, Berlin, Springer-Verlag 1977

    Google Scholar 

  121. Wilcox, D. E., Long, J. R., Solomon, E. I.: to be published

    Google Scholar 

  122. Powers, L. et al.: to be published

    Google Scholar 

  123. Brown, J. M. et al.: J. Am. Chem. Soc. 102, 4210 (1980)

    Article  CAS  Google Scholar 

  124. Co, M. S. et al.: J. Am. Chem. Soc. 103, 984 (1981)

    Article  CAS  Google Scholar 

  125. Hatfield, W. E.: Superexchange interactions in copper(II) complexes, in: Extended Interactions Between Metal Ions in Transition Metal Complexes (ed.) Interrante, L. V., chapter 10, Washington, D. C., ACS, 1974

    Google Scholar 

  126. Coughlin, P. K., Lippard, S. J.: J. Am. Chem. Soc. 103, 3228 (1981)

    Article  CAS  Google Scholar 

  127. Arcus, C., Fivizzani, K. P., Pankovic, S. F.: J. Inorg. Nucl. Chem. 39, 285 (1977)

    Article  CAS  Google Scholar 

  128. Ishimura, Y.: Bull. Chem. Soc. Japan 46, 3728 (1973)

    Article  CAS  Google Scholar 

  129. Loeb, S. J., Martin, J. W. L., Willis, C. J.: Inorg. Chem. 18, 3160 (1979)

    Article  CAS  Google Scholar 

  130. Timmons, J. H. et al.: Inorg. Chem. 20, 181 (1981)

    Article  CAS  Google Scholar 

  131. Curtis, N. F. et al.: J. Chem. Soc. Dalton, 1051 (1977)

    Google Scholar 

  132. Dickson, I. E., Robson, R.: Inorg. Chem. 13, 1301 (1974)

    Article  CAS  Google Scholar 

  133. Countryman, R. M., Robinson, W. T., Sinn, E.: Inorg. Chem. 13, 2013 (1974)

    Article  CAS  Google Scholar 

  134. Harris, C. M., Sinn, E.: J. Inorg. Nucl. Chem. 30, 2723 (1968)

    Article  CAS  Google Scholar 

  135. Gruber, S. J., Harris, C. M., Sinn, E.: J. Inorg. Nucl. Chem. 30, 1805 (1968)

    Article  CAS  Google Scholar 

  136. Goodenough, J. B.: Magnetism and the Chemical Bond, New York, Interscience 1963

    Google Scholar 

  137. Wong, R. Y., Palmer, K. J., Tomimatsu, Y.: Acta. Cryst. B 32, 567 (1976)

    Google Scholar 

  138. Tomimatsu, Y., Kint, S., Scherer, J. R.: Biochemistry 15, 4918 (1976)

    Article  CAS  Google Scholar 

  139. Harrod, J. F.: Canad. J. Chem. 47, 637 (1969)

    Article  CAS  Google Scholar 

  140. Bullock, J. I., Hobson, R. J., Povey, D. C.: J. Chem. Soc. Dalton 2037 (1974)

    Google Scholar 

  141. Ladd, M. F. C., Povey, D. C.: J. Cryst. Mol. Str. 6, 205 (1976)

    Article  CAS  Google Scholar 

  142. Hobson, R. J., Ladd, M. F. C., Povey, D. C.: J. Cryst. Mol. Str 3, 377 (1973)

    Article  CAS  Google Scholar 

  143. Frost, A. E. et al.: J. Am. Chem. Soc. 80, 530 (1958)

    Article  CAS  Google Scholar 

  144. Boggess, R. K., Martin, R. B.: J. Am. Chem. Soc. 97, 3076 (1975)

    Article  CAS  Google Scholar 

  145. Ainscough, E. W., Brodie, A. M., Plowman, J. E.: Inorg. Chim. Acta. 33, 149 (1979)

    Article  CAS  Google Scholar 

  146. Letter, J. E. Jr., Bauman, J. E. Jr.: J. Am. Chem. Soc. 92, 443 (1970)

    Article  CAS  Google Scholar 

  147. Letter, J. E. Jr., Bauman, J. E. Jr.: J. Am. Chem. Soc. 92, 437 (1970)

    Article  CAS  Google Scholar 

  148. Ainscough, E. W. et al.: Biochemistry 19, 4072 (1980)

    Article  CAS  Google Scholar 

  149. The BI component appears to have been observed in the UV-CD difference spectrum of oxy versus met at ∼ 260 nm: K. Lerch, private communication

    Google Scholar 

  150. Thewalt, U., Struckmeier, G.: Z. anorg. allg. Chem. 419, 163 (1976)

    Article  CAS  Google Scholar 

  151. Thewalt, U.: Z. anorg. allg. Chem. 393, 1 (1972)

    Article  CAS  Google Scholar 

  152. Zehnder, M., Thewalt, U., Fallab, S.: Helv. Chim. Acta 59, 2290 (1976)

    Article  CAS  Google Scholar 

  153. Thewalt, U., Marsh, R.: J. Am. Chem. Soc. 89, 6364 (1967)

    Article  CAS  Google Scholar 

  154. Lever, A. B. P., Gray, H. B.: Acc. Chem. Res. 11, 348 (1978)

    Article  CAS  Google Scholar 

  155. Sasaki, Y., Fujita, J., Saito, K.: Bull. Chem. Soc. Japan 44, 3373 (1971)

    Article  CAS  Google Scholar 

  156. Fritch, J. R., Christoph, G. G., Schaefer, W. P.: Inorg. Chem. 12, 2170 (1973)

    Article  CAS  Google Scholar 

  157. Mori, M., Weil, J. A.: J. Am. Chem. Soc. 89, 3732 (1967)

    Article  CAS  Google Scholar 

  158. Thamann, T. J., Solomon, E. I.: to be published

    Google Scholar 

  159. Larrabee, J. A., Spiro, T. G.: J. Am. Chem. Soc. 102, 4217 (1980)

    Article  CAS  Google Scholar 

  160. Reinhammar, B., Malmström, B. G.: “Blue” copper-containing oxidases, in Copper Proteins (ed.) Spiro, T. G., chapter 3, New York, Wiley-Interscience 1981

    Google Scholar 

  161. Reinhammar, B. R. M., Vänngård, T. I.: Eur. J. Biochem. 18, 463 (1971)

    Article  CAS  Google Scholar 

  162. Reinhammar, B.: Biochim. Biophys. Acta 275, 245 (1972)

    Article  CAS  Google Scholar 

  163. Morpurgo, L. et al.: Biochim. Biophys. Acta 336, 324 (1974)

    CAS  Google Scholar 

  164. Farver, O., Goldberg, J., Pecht, I.: Eur. J. Biochem. 104, 71 (1980)

    Article  CAS  Google Scholar 

  165. Graziani, M. T. et al.: FEBS Lett. 70, 87 (1976)

    Article  CAS  Google Scholar 

  166. LuBien, C. D. et al.: J. Am. Chem. Soc. 103, 7014 (1981)

    Article  CAS  Google Scholar 

  167. Thamann, T. J., LuBien, C. D., Solomon, E. I.: to be published

    Google Scholar 

  168. Spira, D. J., Solomon, E. I.: to be published

    Google Scholar 

  169. A half-met laccase kinetic intermediate has also been reported: Reinhammar, B.: J. Inorg. Biochem. 15, 27 (1981)

    Article  CAS  Google Scholar 

  170. Spira, D. J., Co, M. S., Hodgson, K. O., Solomon, E. I.: to be published

    Google Scholar 

  171. Spira, D. J., Winkler, M. E., Solomon, E. I.: Biochem. Biophys. Res. Comm. 107, 721 (1982)

    Article  CAS  Google Scholar 

  172. Winkler, M. E., Spira, D. J., LuBien, C. D., Thamann, T. J., Solomon, E. I.: ibid., 727 (1982)

    CAS  Google Scholar 

  173. LuBien, C. D., Solomon, E. I., Spira, D. J., Thamann, T. J., Winkler, M. E.: manuscript in preparation

    Google Scholar 

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Solomon, E.I., Penfield, K.W., Wilcox, D.E. (1983). Active sites in copper proteins an electronic structure overview. In: Copper, Molybdenum, and Vanadium in Biological Systems. Structure and Bonding, vol 53. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0111302

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  • DOI: https://doi.org/10.1007/BFb0111302

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  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-12042-1

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