Modeling the transition state structures of the xanthine oxidase enzyme active site bound to the thioformate
Key words: thioformate, modeling, transition state, xanthine oxidase.
Anderson, R. F., Hille, R. & Masseyll, V. The Radical Chemistry of Milk Xanthine Oxidase as Studied by Radiation Chemistry Techniques*. 15870–15876 (1986).
Nivorozhkin, A. & Szabo, C. Therapeutic Effects of Xanthine Oxidase Inhibitors : 58, 87–114 (2006).
Rebelo, J. M. & Dias, J. M. Structure re ® nement of the aldehyde oxidoreductase. 791–800 (2001). doi:10.1007/s007750100255
Okamoto, K. et al. The crystal structure of xanthine oxidoreductase during catalysis : Implications for reaction mechanism and enzyme inhibition. 101, 7931–7936 (2004).
Enroth, C., Eger, B. T., Okamoto, K., Nishino, T. & Pai, E. F. Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion. Proc. Natl. Acad. Sci. 97, 10723–10728 (2000).
Beedham, C., Critchley, D.J.P., and Rance, D. . Substrate specificity of human liver aldehyde Oxidase toward substituted quinazolines and phthalazines: a comparison with hepatic enzyme from guinea pig, rabbit, and baboon. 481–90 (1995).
Xia, M., Dempski, R. & Hille, R. The reductive half-reaction of xanthine oxidase. Reaction with aldehyde substrates and identification of the catalytically labile oxygen. J. Biol. Chem. 274, 3323–3330 (1999).
Kessete, J. M. Mechanism of Formate Hydroxylation Catalyzed by Xanthine Oxidase Enzyme. 4, 7–26 (2018).
Yamaguchi, Y., Matsumura, T., Ichida, K. & Okamoto, K. Human Xanthine Oxidase Changes its Substrate Specificity to Aldehyde Oxidase Type upon Mutation of Amino Acid Residues in the Active Site : Roles of Active Site Residues in Binding and Activation of Purine Substrate. 524, 513–524 (2007).
Voityuk, A. A. et al. Substrate Oxidation in the Active Site of Xanthine Oxidase and Related Enzymes. A Model Density Functional Study. (1998). doi:10.1021/ic9707570
Bayse, C. A. Density-functional theory models of xanthine oxidoreductase activity : comparison of substrate tautomerization and protonation †. 2306–2314 (2009). doi:10.1039/b821878a
Bayse, C. A. Theoretical Characterization of the ‘ Very Rapid ’ Mo ( V ) Species Generated in the Oxidation of Xanthine Oxidase. 45, 2199–2202 (2006).
Amano, T., Ochi, N., Sato, H. & Sakaki, S. Oxidation Reaction by Xanthine Oxidase . Theoretical Study of Reaction Mechanism. 9, 8131–8138 (2007).
- There are currently no refbacks.