Matches in SemOpenAlex for { <https://semopenalex.org/work/W2040652904> ?p ?o ?g. }
Showing items 1 to 80 of
80
with 100 items per page.
- W2040652904 endingPage "17617" @default.
- W2040652904 startingPage "17610" @default.
- W2040652904 abstract "Chemical and mutagenic modification combined with X-ray crystallography has been used to probe the ascorbate binding site in ascorbate peroxidase (APX). Chemical modification of the single Cys residue in APX with Ellman's reagent (DTNB) blocks the ability of APX to oxidize ascorbate but not other small aromatic phenolic substrates. DTNB-modified APX (APX-TNB) exhibits only 1.3% wild-type activity when ascorbate is used as the substrate but full activity when aromatic substrates, guaiacol or pyrogallol, are used. Stopped-flow studies show that APX-TNB reacts normally with peroxide to give compound I but that the rates of reduction of both compounds I and II by ascorbate are dramatically slowed. Conversion of Cys32 to Ser leads to approximately 70% drop in ascorbate peroxidase activity with no effect on guaiacol peroxidase activity. These results indicate that uncharged aromatic substrates and the anionic ascorbate molecule interact with different sites on APX. The 2.0 A X-ray crystal structure of APX-TNB shows clear electron density for the TNB group covalently attached to Cys32 in all four molecules of the asymmetric unit, indicating complete and specific modification. It appears that the ascorbate site is blocked by DTNB modification which is well removed from the exposed delta-heme edge where aromatic substrates are thought to bind. This is the first experimental evidence indicating that ascorbate oxidation does not occur at the exposed heme edge but at an alternate binding site in the vicinity of Cys32 near Arg172 and the heme propionates." @default.
- W2040652904 created "2016-06-24" @default.
- W2040652904 creator A5015794500 @default.
- W2040652904 creator A5028937193 @default.
- W2040652904 creator A5059081327 @default.
- W2040652904 date "1998-11-25" @default.
- W2040652904 modified "2023-10-12" @default.
- W2040652904 title "Identification of Two Electron-Transfer Sites in Ascorbate Peroxidase Using Chemical Modification, Enzyme Kinetics, and Crystallography" @default.
- W2040652904 cites W1480657691 @default.
- W2040652904 cites W1528593330 @default.
- W2040652904 cites W2015649222 @default.
- W2040652904 cites W2028231353 @default.
- W2040652904 cites W2049521571 @default.
- W2040652904 doi "https://doi.org/10.1021/bi981958y" @default.
- W2040652904 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9860877" @default.
- W2040652904 hasPublicationYear "1998" @default.
- W2040652904 type Work @default.
- W2040652904 sameAs 2040652904 @default.
- W2040652904 citedByCount "59" @default.
- W2040652904 countsByYear W20406529042012 @default.
- W2040652904 countsByYear W20406529042013 @default.
- W2040652904 countsByYear W20406529042014 @default.
- W2040652904 countsByYear W20406529042015 @default.
- W2040652904 countsByYear W20406529042016 @default.
- W2040652904 countsByYear W20406529042019 @default.
- W2040652904 countsByYear W20406529042021 @default.
- W2040652904 countsByYear W20406529042022 @default.
- W2040652904 countsByYear W20406529042023 @default.
- W2040652904 crossrefType "journal-article" @default.
- W2040652904 hasAuthorship W2040652904A5015794500 @default.
- W2040652904 hasAuthorship W2040652904A5028937193 @default.
- W2040652904 hasAuthorship W2040652904A5059081327 @default.
- W2040652904 hasConcept C130698151 @default.
- W2040652904 hasConcept C162008176 @default.
- W2040652904 hasConcept C178790620 @default.
- W2040652904 hasConcept C181199279 @default.
- W2040652904 hasConcept C184133267 @default.
- W2040652904 hasConcept C185592680 @default.
- W2040652904 hasConcept C2777426643 @default.
- W2040652904 hasConcept C2780199054 @default.
- W2040652904 hasConcept C2986274086 @default.
- W2040652904 hasConcept C31903555 @default.
- W2040652904 hasConcept C538909803 @default.
- W2040652904 hasConcept C55493867 @default.
- W2040652904 hasConcept C71240020 @default.
- W2040652904 hasConceptScore W2040652904C130698151 @default.
- W2040652904 hasConceptScore W2040652904C162008176 @default.
- W2040652904 hasConceptScore W2040652904C178790620 @default.
- W2040652904 hasConceptScore W2040652904C181199279 @default.
- W2040652904 hasConceptScore W2040652904C184133267 @default.
- W2040652904 hasConceptScore W2040652904C185592680 @default.
- W2040652904 hasConceptScore W2040652904C2777426643 @default.
- W2040652904 hasConceptScore W2040652904C2780199054 @default.
- W2040652904 hasConceptScore W2040652904C2986274086 @default.
- W2040652904 hasConceptScore W2040652904C31903555 @default.
- W2040652904 hasConceptScore W2040652904C538909803 @default.
- W2040652904 hasConceptScore W2040652904C55493867 @default.
- W2040652904 hasConceptScore W2040652904C71240020 @default.
- W2040652904 hasIssue "50" @default.
- W2040652904 hasLocation W20406529041 @default.
- W2040652904 hasLocation W20406529042 @default.
- W2040652904 hasOpenAccess W2040652904 @default.
- W2040652904 hasPrimaryLocation W20406529041 @default.
- W2040652904 hasRelatedWork W1979229609 @default.
- W2040652904 hasRelatedWork W2020001094 @default.
- W2040652904 hasRelatedWork W2040652904 @default.
- W2040652904 hasRelatedWork W2042902543 @default.
- W2040652904 hasRelatedWork W2059288054 @default.
- W2040652904 hasRelatedWork W2111692242 @default.
- W2040652904 hasRelatedWork W2113218680 @default.
- W2040652904 hasRelatedWork W2350305086 @default.
- W2040652904 hasRelatedWork W2375459099 @default.
- W2040652904 hasRelatedWork W587135242 @default.
- W2040652904 hasVolume "37" @default.
- W2040652904 isParatext "false" @default.
- W2040652904 isRetracted "false" @default.
- W2040652904 magId "2040652904" @default.
- W2040652904 workType "article" @default.