The oxidation of Octopus vulgaris hemocyanin by nitrogen oxides.

The reaction of Octopus vulgaris hemocyanin with nitrite was studied under a variety of conditions in which the green half-met derivative is formed. Analytical evidence shows that the amount of chemically detectable nitrite in various samples of the derivative is not proportional to the cupric copper detected by EPR. The kinetics of oxidation of hemocyanin as a function of protein concentration and pH, in the presence of nitrite and ascorbate, is consistent with a scheme in which NO2 is the reactive oxidant. We suggest that the green half-methemocyanin contains a metal center with one cuprous and one cupric copper without an exogenous nitrogen oxide ligand.

[1]  J. Tahon,et al.  The reaction of nitrite with the haemocyanin of Astacus leptodactylus. , 1988, The Biochemical journal.

[2]  M. Beltramini,et al.  Emission quenching mechanisms in Octopus vulgaris hemocyanin: steady-state and time-resolved fluorescence studies , 1987 .

[3]  A. Vogel Qualitative Inorganic Analysis , 1987 .

[4]  T. Takagi,et al.  The structure of arthropod hemocyanins. , 1985, Science.

[5]  G. Jori,et al.  The role of copper and quaternary structure on the conformational properties of Octopus vulgaris hemocyanin. , 1984, Archives of biochemistry and biophysics.

[6]  W. Hol,et al.  3.2 Å structure of the copper-containing, oxygen-carrying protein Panulirus interruptus haemocyanin , 1984, Nature.

[7]  B. Kincaid,et al.  Structural studies of the hemocyanin active site. 1. Extended x-ray absorption fine structure (EXAFS) analysis , 1980 .

[8]  B. Salvato,et al.  Hemocyanin of Octopus vulgaris. The molecular weight of the minimal functional subunit in 3 M urea. , 1979, Biochemistry.

[9]  G. Defreyn,et al.  The reaction of nitrogen monoxide and of nitrite with deoxyhaemocyanin and methaemocyanin of Helix pomatia. , 1979, European journal of biochemistry.

[10]  E. Solomon,et al.  Comparison of half-met and met apo hemocyanin. Ligand bridging at the binuclear copper active site , 1979 .

[11]  E. Solomon,et al.  Spectroscopic studies of ligand perturbation effects on the half oxidized action site of Busycon canaliculatum hemocyanin. , 1978, Biochemical and biophysical research communications.

[12]  H. van der Deen,et al.  Nitrite and nitric oxide treatment of Helix pomatia hemocyanin: single and double oxidation of the active site. , 1977, Biochemistry.

[13]  T. J. Thamann,et al.  Resonance Raman study of oxyhemocyain with unsymmetrically labeled oxygen. , 1977, Journal of the American Chemical Society.

[14]  T. B. Freedman,et al.  A resonance Raman study of the copper protein, hemocyanin. New evidence for the structure of the oxygen-binding site. , 1976, Journal of the American Chemical Society.

[15]  B. Salvato,et al.  A circular dichroism study of some hemocyanins. , 1976, Comparative biochemistry and physiology. B, Comparative biochemistry.

[16]  M. Frisse,et al.  Nitrosylmetalloporphyrins. II. Synthesis and molecular stereochemistry of mitrosyl-alpha, beta, gamma, delta,-tetraphenylporphinatoiron (ii) , 1975, Journal of the American Chemical Society.

[17]  B. Salvato,et al.  Acid-base titration of hemocyanin from Octopus vulgaris Lam. , 1974, Biochemistry.

[18]  A. J. Uiterkamp,et al.  Monomer and magnetic dipole‐coupled Cu2+ EPR signals in nitrosylhemocyanin , 1972, FEBS letters.

[19]  I. M. Klotz,et al.  Oxygen-carrying proteins: a comparison of the oxygenation reaction in hemocyanin and hemerythrin with that in hemoglobin. , 1955, Science.