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Insights into the catalytic mechanism of synthetic glutathione peroxidase mimetics.
Bhowmick, Debasish; Mugesh, Govindasamy.
Afiliación
  • Bhowmick D; Department of Inorganic and Physical Chemistry, Indian Institute of Science, Bangalore 560 012, India. mugesh@ipc.iisc.ernet.in.
Org Biomol Chem ; 13(41): 10262-72, 2015 Nov 07.
Article en En | MEDLINE | ID: mdl-26372527
Glutathione Peroxidase (GPx) is a key selenoenzyme that protects biomolecules from oxidative damage. Extensive research has been carried out to design and synthesize small organoselenium compounds as functional mimics of GPx. While the catalytic mechanism of the native enzyme itself is poorly understood, the synthetic mimics follow different catalytic pathways depending upon the structures and reactivities of various intermediates formed in the catalytic cycle. The steric as well as electronic environments around the selenium atom not only modulate the reactivity of these synthetic mimics towards peroxides and thiols, but also the catalytic mechanisms. The catalytic cycle of small GPx mimics is also dependent on the nature of peroxides and thiols used in the study. In this review, we discuss how the catalytic mechanism varies with the substituents attached to the selenium atom.
Asunto(s)

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Materiales Biomiméticos / Glutatión Peroxidasa Idioma: En Revista: Org Biomol Chem Año: 2015 Tipo del documento: Article País de afiliación: India

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Materiales Biomiméticos / Glutatión Peroxidasa Idioma: En Revista: Org Biomol Chem Año: 2015 Tipo del documento: Article País de afiliación: India