Superoxide dismutase structural

Hart, P.J. (2006) Pathogenic superoxide dismutase structure, folding, aggregation and turnover, Curr. Opin. Chem. Biol., 10, 131-138. 

McCord, J. M. Iron- and manganese containing superoxide dismutases Structure, distribution, and evolutionary relationships. In Iron and Copper Proteins (Yasunobu, K. T., Mower, H. F., Hayaishi, O., eds.), New York-London, Plenum Press, 1976, pp. 540-550... 

Klapper 1, R Hagstrom, RFine, K Sharp and B Honig 1986. Focusing of Electric Fields in tire Actir e Sit of CuZn Superoxide Dismutase Effects of Ionic Strength and Amino-Acid Substitution. Proteins Structure, Function and Genetics 1 47-59. 

Figure S.l The enzyme superoxide dismutase (SOD). SOD is a P structure comprising eight antiparallel P strands (a). In addition, SOD has two metal atoms, Cu and Zn (yellow circles), that participate in the catalytic action conversion of a superoxide radical to hydrogen peroxide and oxygen. The eight p strands are arranged around the surface of a barrel, which is viewed along the barrel axis in (b) and perpendicular to this axis in (c). [(a) Adapted from J.S. Richardson. The stmcture of SOD was determined in the laboratory of J.S. and D.R. Richardson, Duke University.)...

Tainer, J.A., et al. Determination and analysis of the 2 A structure of copper, zinc superoxide dismutase. 

Structure and Properties of Copper-Zinc Superoxide Dismutases Ivano Bertini, Stefano Mangani, and Maria Silvia Viezzoli... 

The structure of the enzymatic site of superoxide dismutase. The proximity, with a histidine side chain (color screened) acting as a bridge between the metals. 

Wuerges J, J-W Lee, Y-I Yim, H-S Yrm, S-O Kang, KD Carugo (2004) Crystal structure of nickel-containing superoxide dismutase reveals another type of active site. Proc Natl Acad Sci USA 101 8569-8574. 

Nickel is found in thiolate/sulflde environment in the [NiFe]-hydrogenases and in CODH/ACS.33 In addition, either a mononuclear Ni-thiolate site or a dinuclear cysteine-S bridged structure are assumed plausible for the new class of Ni-containing superoxide dismutases, NiSOD (A).34 [NiFe]-hydrogenase catalyzes the two-electron redox chemistry of dihydrogen. Several crystal structures of [NiFe]-hydrogenases have demonstrated that the active site of the enzyme consists of a heterodinuclear Ni—Fe unit bound to thiolate sulfurs of cysteine residues with a Ni—Fe distance below 3 A (4) 35-39 This heterodinuclear active site has been the target of extensive model studies, which are summarized in Section 6.3.4.12.5. 

Imidazoles are of interest as bridging ligands particularly with regard to mimics of the active site of Cu-Zn superoxide dismutase (SOD). Structures with imidazolate bridges have been... 

Carloni et al.91 applied the DFT(PZ) calculations to investigate the electronic structure of various models of oxydized and reduced Cu, Zn superoxide dismutase. The first stage of the enzymatic reaction involves the electron transfer from Cu" ion to superoxide. The theoretical investigations provided a detailed description of the electronic structure of the molecules involved in the electron transfer process. The effect of charged groups, present in the active center, on the electron transfer process were analyzed and the Argl41 residue was shown to play a crucial role. 

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. 

One last class of mononuclear non-haem iron enzyme that we have not yet considered, consists of the microbial superoxide dismutases with Fe(III) at their active site. The crystal structure of the E. coli enzyme shows a coordination geometry reminiscent of protocatechuate 3,4-dioxygenase, with four endogenous protein ligands, three His and one Asp residue, and one bound water molecule (Carlioz et ah, 1988). 

M.E. Schinia, L. Maffey, D. Barra, F. Bossa, K. Puget, and A.M. Michelson, The primary structure of iron superoxide dismutase from Escherichia coli. FEBS Lett. 221, 87-90 (1987). 

D. Ringe, G.A. Petsko, F. Yamakura, K. Suzuki, and D. Ohmori, Structure of iron superoxide dismutase from Pseudomonas ovalis at 2.9. ANG. resolution. Proc. Natl. Acad. Sci. U.SA. 80, 3879-3883 (1983). 

W.C. Stallings, C. Bull, J.A. Fee, M.S. Lah, and M.L. Ludwig, Iron and manganese superoxide dismutases catalytic inferences from the structures. Current Communications in Cell Molecular Biology. 5, 193-211 (1992). 

A. Carlioz, M.L. Ludwig, W.C. Stallings, J.A. Fee, H.M. Steinman, and D. Touati, Iron superoxide dismutase. Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures. J. Biol. Chem. 263, 1555-1562 (1988). 

B.L. Stoddard, P.L. Howell, D. Ringe, and G.A. Petsko, The 2.1. ANG. resolution structure of iron superoxide dismutase from Pseudomonas ovalis. Biochemisry. 29, 8885-8893 (1990). 

M.L. Ludwig, A.L. Metzger, K.A. Pattridge, and W.C. Stallings, The structure of iron superoxide dismutase from Pseudomonas ovalis complexed with the inhibitor azide. J. Mol. Biol. 219, 335-358 (1991). 

Structure-Activity Studies and the Design of Synthetic Superoxide Dismutase (SOD) Mimetics as Therapeutics... 

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