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E. ). New York: Academic Press 1966. 26. Brooks, D. , Dawson, C. : In: The biochemistry of copper, p. 343 (J. Peisaeh, P. Aisen and W. E. ). New York: Academic Press 1966. 27. Kertesz, D. : In: The biochemistry of copper, p. 359 (J. Peisaeh, P. Aisen and W. E. ). New York: Academic Press 1966. 28. Levine, W. : In: The biochemistry of copper, p. 371 (J. Peisaeh, P. Aisen and W. E. ). New York: Academic Press 1966. 29. , Ogura, Y. : In: The biochemistry of copper, p. 389 (J. Peisaeh, P. Aisen and W.

J Fig. 29. Possible substrate complex for erythrocuprein Thanks to its electron affinity, oxygen is able to accept up to four electrons (Fig. 9). The electrons are filling the empty a* molecular orbital and the halffilled ~* molecular orbitals. As the number of electrons increases, the 0 - 0 distances are progressively increased, finally causing dissociation. In Fig. 29 the substrate specificity of 0~. for erythrocuprein should be critically examined. Considering the fact that erythrocuprein reacts extremely fast (,--2 × 109 M-1 s -1 ((82) with O~.

Aisen and W. E. ). New York: Academic Press 1966. 41. , McDermott, dr. , drohnson, D. , Frieden, E. : In : The biochemistry of copper, p. 559 (J. Peisach, P. Aisen and W. E. ). New York: Academic Press 1966. 42. Redfield, A. C. : The Haemocyanins. Biol. Rev. 9, 176 (1934). 43. -- Haemocyanin in "Copper Metabolism: A Symposium on Animal, Plant and Soil Relationships", p. 174. Baltimore, Maryland: Johns Hopkins Press 1950. 44. , McDermott, dr. , Osahi, S. : Oxidases and related redox systems, p. 240.

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