Haloperoxidase model compounds

SCHEME 10.5 Hydrogen bond between one peroxo oxygen and a hydrogen of the amino group. 

SCHEME 10.6 Ligands used with hydrogen peroxide as models of peroxidase activity. 

Gresser, M.J., A.S. Tracey, and N.D. Chasteen. 1990. Vanadates as phosphate analogs in biochemistry. Vanadium in biological systems. Dordrecht, Boston, London Kluwer Academic Publishers, pp 63-79. 

Gaidamauskas, and L. Yang. 2004. The chemistry and biochemistry of vanadium and the biological activities exerted by vanadium compounds. Chem. Reviews 104 849-902. 

Pettersson, L., B. Hedman, A.M. Nenner, and I. Andersson. 1985. Multicomponent polyanions. 36. Hydrolysis and redox equilibria of the II+-I IV()42 system in 0.6 M Na(Cl). A complementary potentiometric and 51-V NMR study at low vanadium concentrations in acid solution. Acta Chem. Scand. 39 499-506. 

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This book does not follow a chronological sequence but rather builds up in a hierarchy of complexity. Some basic principles of 51V NMR spectroscopy are discussed this is followed by a description of the self-condensation reactions of vanadate itself. The reactions with simple monodentate ligands are then described, and this proceeds to more complicated systems such as diols, -hydroxy acids, amino acids, peptides, and so on. Aspects of this sequence are later revisited but with interest now directed toward the influence of ligand electronic properties on coordination and reactivity. The influences of ligands, particularly those of hydrogen peroxide and hydroxyl amine, on heteroligand reactivity are compared and contrasted. There is a brief discussion of the vanadium-dependent haloperoxidases and model systems. There is also some discussion of vanadium in the environment and of some technological applications. Because vanadium pollution is inextricably linked to vanadium(V) chemistry, some discussion of vanadium as a pollutant is provided. This book provides only a very brief discussion of vanadium oxidation states other than V(V) and also does not discuss vanadium redox activity, except in a peripheral manner where required. It does, however, briefly cover the catalytic reactions of peroxovanadates and haloperoxidases model compounds. 

Professor M. R. Maurya is currently heading the Department of Chemistry, IIT Roorkee. He has more than 26 years of teaching and research experience. He had worked in Loyola University of Chicago, USA, Iowa State University, Ames, Iowa, USA, National Chemical Laboratory, Pune, and Pune University Pune, before joining department of Chemistry at IIT Roorkee in 1996 and became full professor in 2008. His current area of research interests include structural and functional models of vanadate-dependent haloperoxidases, coordination polymers and their catalytic study, metal complexes encapsulated in zeolite cages and their catalytic study, polymer-anchored metal complexes and their catalytic study, and medicinal aspects of coordination compounds. So far, he has guided 21 doctoral and 7 Master s theses, co-authored more than 140 research papers in the international refereed journals. 

Conte, V., O. Bortolini, M. Carraro, and S. Moro. 2000. Models for the active site of vanadium-dependent haloperoxidases Insight into the solution structure of peroxo-vanadium compounds. J. Inorg. Biochem. 80 41 -9. 

Many peroxovanadates have potent insulin-mimetic properties [1,2]. Apparently, this functionality derives from the ability of these compounds to rapidly oxidize the active site thiols found in the group of protein tyrosine phosphatases that are involved in regulating the insulin receptor function [3], The discovery of vanadium-dependent haloperoxidases in marine algae and terrestrial lichens provided an additional stimulus in research toward obtaining functional models of peroxidase activity, and there is great interest in duplicating the function of these enzymes (see Section 10.4.2). 

Guevara-Garcia, J.A., N. Barba-Behrens, R. Contreras, and G. Mendosa-Diaz. 1998. Bis-peroxo-oxovanadium(V) complexes of histidine-containing peptides as models for vanadium haloperoxidases. In Vanadium Compounds Chemistry, Biochemistry and Therapeutic Applications. A.S. Tracey and D.C. Crans (Eds). American Chemical Society, Washington, D.C. 126-35. 

Naturally Occurring Vanadium Compounds 4.3.3.1 Structural Models of Reduced Haloperoxidases... 

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