Enzymatická a neenzymatická dehalogenace 1,2-chloroethanu a 1,2-dibromoethanu

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F04%3A00002220" target="_blank" >RIV/61989592:15310/04:00002220 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Enzymatic and Nonenzymatic Dehalogenation of 1,2-chloroethane and 1,2-dibromoethane

Popis výsledku v původním jazyce

1,2-Dichloroethane (DCE) and 1,2-dibromoethane (DBE) are toxic and mutagenic halogenated compounds. As many other synthetic halogenated aliphatic compounds, both are rather resistant to biodegradation and persist in the environment1. Nevertheless, several bacterial cultures that are able to use DCE as the only carbon and halogen source have been isolated. The most efficient catalysis has been observed with the haloalkane dehalogenase DhlA from Xanthobacter autotrophicus GJ10 and substantially low activity with haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT262. A crystallographic analysis of LinB-DCE complex showed non-productive binding of DCE to the enzyme active site, while molecular docking suggested that DCE molecule can possibly bind to the active site but is prevented by chloride ion and/or water molecules3. The different reactivity of DCE and DBE was examined by quantum mechanical calculations as well as by molecular dynamics simulations of enzyme-substrate compl

Název v anglickém jazyce

Enzymatic and Nonenzymatic Dehalogenation of 1,2-chloroethane and 1,2-dibromoethane

Popis výsledku anglicky

1,2-Dichloroethane (DCE) and 1,2-dibromoethane (DBE) are toxic and mutagenic halogenated compounds. As many other synthetic halogenated aliphatic compounds, both are rather resistant to biodegradation and persist in the environment1. Nevertheless, several bacterial cultures that are able to use DCE as the only carbon and halogen source have been isolated. The most efficient catalysis has been observed with the haloalkane dehalogenase DhlA from Xanthobacter autotrophicus GJ10 and substantially low activity with haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT262. A crystallographic analysis of LinB-DCE complex showed non-productive binding of DCE to the enzyme active site, while molecular docking suggested that DCE molecule can possibly bind to the active site but is prevented by chloride ion and/or water molecules3. The different reactivity of DCE and DBE was examined by quantum mechanical calculations as well as by molecular dynamics simulations of enzyme-substrate compl

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2004

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Acta Universitatis Palackianae Olomucensis, Facultas Rerum Naturalium, Chemica

ISSN

0232-0061

e-ISSN

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Svazek periodika

43

Číslo periodika v rámci svazku

Suppl.

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

275

Strana od-do

261-262

Kód UT WoS článku

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EID výsledku v databázi Scopus

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