Superoxide dismutase interactions

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

Carloni, P., P. E. Blochl, and M. Parrinello. 1995. Electronic Structure of the Cu, Zn Superoxide Dismutase Active Site and Its Interactions with the Substrate. J. Phys. Chem. 99, 1338. 

Most proteins contain more than one polypeptide chain. The manner in which these chains associate determines quaternary structure. Binding involves the same types of noncovalent forces mentioned for tertiary structure van der Waals forces, hydrophobic and hydrophilic attractions, and hydrogen bonding. However, the interactions are now interchain rather than infrachain (tertiary structure determination). The quaternary structure of hemoglobin (four almost identical subunits) will be discussed in Chapter 4, that of superoxide dismutase (two identical subunits) will be discussed in Chapter 5, and that of nitrogenase (multiple dissimilar subunits) will be discussed in Chapter 6. 

Carloni, P., Blochl, P. E. and Parrinello, M. Electronic structure of the Cu,Zn superoxide dismutase active site and its interactions with the substrate, J.Phys.Chem., 99 (1995), 1338-1348... 

Thus, superoxide can react with almost all redox-active metal centers (Scheme 1). In general, going through similar redox reaction steps metal complexes can interact with superoxide either as catalysts for its dismutation (superoxide dismutase (SOD) mimetics), or in a stoichiometric manner (Scheme 1). 

A representative sampling of non-heme iron proteins is presented in Fig. 3. Evident from this atlas is the diversity of structural folds exhibited by non-heme iron proteins it may be safely concluded that there is no unique structural motif associated with non-heme iron proteins in general, or even for specific types of non-heme iron centers. Protein folds may be generally classified into several categories (i.e., all a, parallel a/)3, or antiparallel /8) on the basis of the types and interactions of secondary structures (a helix and sheet) present (Richardson, 1981). Non-heme iron proteins are found in all three classes (all a myohemerythrin, ribonucleotide reductase, and photosynthetic reaction center parallel a/)8 iron superoxide dismutase, lactoferrin, and aconitase antiparallel )3 protocatechuate dioxygenase, rubredoxins, and ferredoxins). This structural diversity is another reflection of the wide variety of functional roles exhibited by non-heme iron centers. 

The electrochemical properties of immobilized copper, zinc superoxide dismutase, and their interaction with super oxide radicals were investigated [474]. 

The applicability of CE-ICP-MS for fast screening of weak metal interactions of Cd2+ with several test proteins (such as carbonic anhydrase from bovine erythrocytes, bovine serum albumin, human holotransferrin, ceruloplasmin and superoxide dismutase) has been studied by Cahmoun and Hagege.74 The sensitivity of element species and their detection limits in CE-ICP-MS have been improved by introducing a preconcentration step involving large volume stacking with polarity... 

O Neill, P., Fielden, E. M. Pulse radiolysis investigation of the interaction of bovine superoxide dismutase with organic free radicals. In Chemical and Biochemical Aspects of Superoxide and Superoxide Dismutase (Bannister, J. V., Hill, H. A. O., eds.). New York-Amsterdam-Oxford, Elsevier/North-Holland, 1980, pp. 357-363... 

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