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'Thermodynamic' mechanism of catalysis by haloperoxidases

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dc.contributor.author Shevelkova A.
dc.contributor.author Sal'nikov Y.
dc.contributor.author Kuz'mina N.
dc.contributor.author Ryabov A.
dc.date.accessioned 2018-09-17T20:12:45Z
dc.date.available 2018-09-17T20:12:45Z
dc.date.issued 1996
dc.identifier.issn 0014-5793
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/133188
dc.description.abstract A novel 'thermodynamic' mechanistic rationale of haloperoxidase catalysis is based on the following two assumptions: (i) the role of enzyme consists only in the rapid equilibration between the halogen-containing species originating from halide and hydrogen peroxide; (ii) the interaction between the enzyme and organic substrate is kinetically insignificant and halogenation occurs as a result of the electrophilic attack of the active brominating (Br3 -, Br2 and HBrO) or chlorinating (HClO) species at monochlorodimedon indicative of a higher chloride 'specificity' of chloroperoxidase from C. fumago.
dc.relation.ispartofseries FEBS Letters
dc.subject Catalysis
dc.subject Haloperoxidase
dc.subject Mechanism
dc.title 'Thermodynamic' mechanism of catalysis by haloperoxidases
dc.type Article
dc.relation.ispartofseries-issue 3
dc.relation.ispartofseries-volume 383
dc.collection Публикации сотрудников КФУ
dc.relation.startpage 259
dc.source.id SCOPUS00145793-1996-383-3-SID0029935176


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  • Публикации сотрудников КФУ Scopus [24551]
    Коллекция содержит публикации сотрудников Казанского федерального (до 2010 года Казанского государственного) университета, проиндексированные в БД Scopus, начиная с 1970г.

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