Cops and robbers: Putative evolution of copper oxygen-binding proteins

Journal of Experimental Biology

Volumn 203, Issue 12, 2000, Pages 1777-1782

  Decker, Heinz ^a   Terwilliger, Nora ^b  

^a JOHANNES GUTENBERG UNIVERSITY   (Germany)

^b UNIVERSITY OF OREGON   (United States)

Author keywords

Copper oxygen binding protein; Evolution; Haemocyanin; Immune response; Oxygen transport; Phenoloxidase

Indexed keywords

COPPER; HEMOCYANIN; MONOPHENOL MONOOXYGENASE; OXYGEN;

ANIMAL; ARTICLE; BINDING SITE; CHEMISTRY; METABOLISM; MOLECULAR EVOLUTION;

ANIMALS; BINDING SITES; COPPER; EVOLUTION, MOLECULAR; HEMOCYANIN; MONOPHENOL MONOOXYGENASE; OXYGEN;

ANIMALIA;

EID: 0033922612     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (50)

1. Anderson, S. O. (1991). Sclerotization of insect cuticle. In Molting and Metamorphosis (ed. E. Ohnishi and H. Ishizaki), pp. 133-155. Tokyo: Japan Science Society Press; Berlin: Springer-Verlag.
2. Ashida, M. and Yamazaki, H. I. (1990). Biochemistry of the phenoloxidase system in insects: with special reference to its activation. In Molting and Metamorphosis (ed. E. Ohnishi and H. Ishizaki), pp. 239-265. Tokyo: Japan Science Society Press; Berlin: Springer-Verlag.
3. Aspan, A., Huang, T. S., Cerenius, L. and Soderhall, K. (1995). cDNA cloning of prophenoloxidase from the freshwater crayfish Pacifastacus leniusculus and its activation. Proc. Natl. Acad. Sci. USA 92, 939-943.
4. Barret, F. M. (1991). Phenoloxidases and the integument. In Physiology of the Insect Epidermis (ed. K. Binnington and A. Retnakaran), pp. 195-212. Melbourne: CSIRO Publishers.
5. - with the binuclear copper site of Neurospora tyrosinase: its relevance for a comparison between tyrosinase and hemocyanin active sites. Biochim. Biophys. Acta 1040, 365-372.
6. Bhagvat, H. and Richter, D. (1938). Animal phenolases and adrenaline. Biochem. J. 32, 1397-1405.
7. Burmester, T. and Scheller, K. (1996). Common origin of arthropod tyrosinase, arthropod hemocyanin, insect hexamerin, and dipteran arylphorin receptor. J. Mol. Evol. 42, 713-728.
8. Cuff, M. E., Miller, K. I., van Holde, K. and Hendricksen, W. A. (1998). Crystal structure of a functional unit from Octopus dofleini hemocyanin. J. Mol. Biol. 278, 855-870.
9. Decker, H. and Rimke, T. (1998). Tarantula hemocyanin shows phenoloxidase activity. J. Biol. Chem. 273, 25889-25892.
10. Drexel, R., Siegmund, S., Schneider, H.-J., Linzen, B., Gielens, C., Preaux, G., Kellerman, J. and Lottspeich, F. (1987). Complete amino acid sequence of a functional unit from molluscan hemocyanin (Helix pomatia). Biol. Chem. Hoppe-Seyler 368, 617-635.
11. Durstewitz, G. and Terwilliger, N. B. (1997). cDNA cloning of a developmentally regulated hemocyanin subunit in the crustacean Cancer magister and phylogenetic analysis of the hemocyanin gene family. Mol. Biol. Evol. 14, 266-276.
12. Fujimoto, K., Okino, N., Kawabata, S., Iwanaga, S. and Ohnishi, E. (1995). Nucleotide sequence of the cDNA encoding the proenzyme of phenol oxidase A1 of Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 92, 7769-7773.
13. Hazes, B., Magnus, K. A., Bonaventura, C., Bonaventura, J., Dauter, Z., Kalk, K. H. and Hol, W. G. J. (1993) Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation. Protein Sci. 2, 597-619.
14. Himmelwright, R. S., Eickman, N. C., LuBien, C. C., Lerch, K. and Solomon, E. I. (1980). Chemical and spectroscopic studies of the binuclear copper active site of Neurospora tyrosinase: comparison to hemocyanins. J. Am. Chem. Soc. 102, 7339-7345.
15. Inaba, T. and Funatsu, M. (1964). Studies on tyrosinase in the housefly. III. Activation of protyrosinase by natural activator. Science 148, 964-965.
16. Jiang, H., Wang, Y., Ma, C. and Kanost, M. R. (1997). Subunit composition of pro-phenol oxidase from Manduca sexta: Molecular cloning of subunit ProPO-P1. Insect Biochem. Mol. Biol. 27, 835-850.
17. Jolly, R. L., Evans, L. H. and Mason, H. S. (1972). Reversible oxygenation of tyrosinase. Biochem. Biophys. Res. Commun. 46, 878-884.
18. Kitajima, N. and Morooka, Y. (1994). Copper-dioxygen complexes. Inorganic and bioinorganic perspectives. Chem. Rev. 94, 737-757.
19. Klabunde, T., Eicken, C., Sacchettini, J. C. and Krebs, B. (1998). Crystal structure of a plant catechol oxidase containing a dicopper center. Nature Structure Biology 5, 1084-1090.
20. Kuiper, H. A., Finazzi-Agro, A., Antonini, E. and Brunori, M. (1980). Luminescence of carbon monoxide hemocyanins. Proc. Natl. Acad. Sci. USA 77, 2387-2389.
21. Lerch, K. (1981). Tyrosinase. In Metal Ions in Biological Systems, vol. B (ed. H. Sigel), pp. 143-186. New York: Dekker.
22. Lerch, K. (1987). Protein and active-site structure of tyrosinase. Prog. Clin. Biol. Res. 256, 85-98.
23. Ling, J., Nestor, L. P., Czernuszewicz, R. S., Spiro, T. G., Fraczkiewicz, R., Sharma, K. D., Loehr, T. M. and Sanders-Loehr, J. (1994). Common oxygen binding site in hemocyanins from arthropods and molluscs: Evidence from Raman spectroscopy and normal coordinate analysis. J. Am. Chem. Soc. 116, 7682-7691.
24. Magnus, K. A., Hazes, B., Ton-That, H., Bonaventura, C., Bonventura, J. and Hol, W. G. J. (1994). Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences. Proteins Struct. Funct. Genet. 19, 302-309.
25. Markl, J. and Decker, H. (1992). Molecular structure of arthropodan hemocyanins. Adv. Comp. Env. Physiol. 13, 325-376.
26. Mason, H. S. (1955). Comparative biochemistry of the phenolase complex. Adv. Enzymol. 16, 105-184.
27. Miller, K. I., Cuff, M. E., Lang, W. F., Varga-Weisz, P., Field, K. G. and van Holde, K. (1998). Sequence of the Octopus dofleini hemocyanin subunit: structural and evolutionary implications. J. Mol. Biol. 278, 827-841.
28. Moore, B. M. and Flurkey, W. H. (1990). Sodium dodecyl sulfate activation of a plant polyphenoloxidase. Effect of sodium dodecyl sulfate on enzymatic and physical characteristics of purified broad bean polyphenoloxidase. J. Biol. Chem. 265, 4982-4988.
29. Nakahara, A., Suzuki, S. and Kino, J. (1983). Tyrosinase activity of squid hemocyanin. Life Sci. Rep. (Suppl.) 1, 319-322.
30. Prota, G. (1992). Melanins and Melanogenesis. San Diego: Academic Press.
31. Salvato, B. and Beltramini, M. (1990). Hemocyanin molecular architecture: Structure and reactivity of the binuclear copper site. Life Chem. Rep. 8, 1-47.
32. Salvato, B., Jori, G., Piazzese, A., Ghiretti, F., Beltramini, M. and Lerch, K. (1983). Enzymatic activities of type-3 copper pair in Octopus vulgaris haemocyanin. Life Sci. Rep. (Suppl.) 1, 313-317.
33. Salvato, B., Santamaria, M., Beltramini, M., Alzuet, G. and Casella, L. (1998). The enzymatic properties of hemocyanins: The o-diphenol oxidase activity. Biochemistry 37, 14065-14077.
34. Sanchez-Ferrer, A., Rodriguez-Lopez, J. N., Garcia-Canovas, F. and Garcia-Carmona, F. (1995). Tyrosinase: A comprehensive review of its mechanism. Biochim. Biophys. Acta 1247, 1-11.
35. Smith, V. J. and Söderhäll, K. (1991). A comparison of phenoloxidase activity in the blood of marine invertebrates. Dev. Comp. Immunol. 15, 251-261.
36. Söderhäll, K. and Cerenius, L. (1998). Role of the prophenoloxidase-activating system in invertebrate immunity. Curr. Opin. Immunol. 10, 23-28.
37. Solomon, E. I., Sundaram, U. M. and Mackonkin, T. E. (1996). Multicopper oxygenases and oxygenases. Chem. Rev. 96, 2563-2605.
38. Solomon, E. I., Tuczek, F., Root, D. E. and Brown, C. A. (1994). Spectroscopy of binuclear dioxygen complexes. Chem. Rev. 94, 827-856.
39. Sugamaran, M. (1990). Prophenoloxidase activation and insect immunity. UCLA Symp. Mol. Cell. Biol. 121, 47-62.
40. Sugumaran, M. and Kanost, M. (1993). Regulation of insect hemolymph phenoloxidases. In Parasites and Pathogens of Insects (ed. N. E. Beckage, S. N. Thompson and A. B. Federici), pp. 317-342. San Diego: Academic Press.
41. Terwilliger, N. (1998). Functional adaptations of oxygen-transport proteins. J. Exp. Biol. 201, 1085-1098.
42. Terwilliger, N., Dangott, L. and Ryan, M. (1999). Cryptocyanin, a crustacean molting protein: Evolutionary link with arthropod hemocyanins and insect hexamerins. Proc. Natl., Acad. Sci. USA 96, 2013-2018.
43. van Gelder, C. W. G., Flurkey, W. H. and Wicherts, H. J. (1997). Sequence and structural features of plant and fungal tyrosinases. Phytochem. 45, 1309-1323.
44. van Heel, M. and Dube, P. (1994). Quaternary structure of multimeric arthropod hemocyanins. Micron 25, 387-418.
45. van Holde, K. E. (1998). Respiratory proteins of invertebrates: Structure, function and evolution. Zoology 100, 287-297.
46. van Holde, K. E. and Miller, K. I. (1982). Hemocyanins. Q. Rev. Biophys. 15, 1-129.
47. van Holde, K. E. and Miller, K. I. (1995). Hemocyanins. Adv. Prot. Chem. 47, 1-81.
48. Volbeda, A. and Hol, W. G. J. (1989a). Crystal structure of hexameric hemocyanin from Panulirus interrupts refined at 3 Å. J. Mol. Biol. 209, 249-279.
49. Volbeda, A. and Hol, W. G. J. (1989b). Pseudo 2 fold symmetry in the copper-binding domain of arthropodan haemocyanin. J. Mol. Biol. 209, 531-546.
50. Zlateva, T., di Muro, P., Salvato, B. and Beltramini, M. (1996). The o-diphenol oxidase activity of arthropod hemocyanin. FEBS Lett. 384, 251-254.