Bovine erythrocyte superoxide dismutase

Hodgson, E.K. and Friedovich, I. (1975). The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide Chemiluminescence and peroxidation. 

J.S. Valentine, M.W. Pantoliano, PJ. Mcdonnell, A.R. Burger, and S.J. Lippard, pH-dependent migration of copper(II) to the vacant zinc-binding site of zinc-free bovine erythrocyte superoxide dismutase. Proc. Natl. Acad. Sci. U.S.A. 76, 4245-4249 (1979). 

J.A. Fee, R. Natter, and G.S.T. Baker, Reconstitution of bovine erythrocyte superoxide dismutase. II. Observations on the nature of catalyzed superoxide. Biochim. Biophy. Acta. 295, 96-106 (1973). 

M. Borsari and H.A. Azab, Voltammetric behavior of bovine erythrocyte superoxide dismutase. Bioelectrochem. Bioenerg. 27, 229-233 (1992). 

J.A. Fee and P.E. DiCorleto, Oxidation-reduction properties of bovine erythrocyte superoxide dismutase. Biochemistry. 12, 4893-4899 (1973). 

Enzymes and Coenzymes Electrochemical behavior of bovine erythrocyte superoxide dismutase adsorbed on Hg electrode has been studied by Qian... 

Lippard, S. J. et al. Physical and chemical studies of bovine erythrocyte superoxide. dismutase. In Bioinorganic Chemistry II (Raymond, K. N., ed.), Washington, DC, Adv. Chem. Series 162, Amer. Chem. Soc., 1977, pp. 251-261... 

Malinowski D. P. Fridovich I. Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase. Biochemistry 1979, 18, 5908-5916. 

Sette, M., Paci, M., Desideri, A. and Rotillo, G. (1992) Formate as an NMR probe of anion binding to copper-zinc and copper-cobalt bovine erythrocyte superoxide dismutase. Biochemistry, 31, 2410-2415. 

Physical and Chemical Studies of Bovine Erythrocyte Superoxide Dismutase... 

The structure and enzyme kinetics of bovine erythrocyte superoxide dismutase are reviewed. The protein has a novel imidazolate-bridged copper(II)-zinc(II) catalytic center in each of two identical subunits. Since a C /Cu1 redox couple is responsible for the dismutase activity of the enzyme, the role of zinc is of interest. Both 220-MHz NMR measurements of the exchangeable histidine protons and chemical modifications using diethylpyrocarbonate demonstrate that zinc alone can fold the protein chain in the region of the active site into a conformation resembling that of the native enzyme. Other possible roles for zinc are discussed. Synthetic, magnetic, and structural studies of soluble, imidazolate-bridged copper complexes of relevance to the 4 Cu(II) form of the enzyme have been made. 

HP here is great interest in the biochemistry and relevant coordination chemistry of copper-containing proteins (1,2, 3, 4, 5). They are widely distributed in both plants and animals and are often involved in oxygen metabolism, transport, and use. One of the most actively studied copper proteins is bovine erythrocyte superoxide dismutase (SOD) (6,7,8). This enzyme catalyzes the dismutation of superoxide ion, Reaction 1. 

Cudd A, Fridovich I. (1982) Electrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase. /Biol Chem 257 11443-11447. 

Superoxide dismutation bovine erythrocyte superoxide dismutase O2 removal (dismutation)... 

Figure 99 The molecular structure of bovine erythrocyte superoxide dismutase ...

Previously, the charge isomers of aqueously isolated bovine erythrocyte superoxide dismutase were separated and subjected to many biophysical investigations including the comparison with the enzymes isolated by the Tsushihashi-procedure Amino... 

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