Matches in SemOpenAlex for { <https://semopenalex.org/work/W2043284578> ?p ?o ?g. }
- W2043284578 endingPage "247" @default.
- W2043284578 startingPage "243" @default.
- W2043284578 abstract "Adhesive proteins secreted by the marine mussel could bind strongly to all kinds of surfaces, for instance, ship hulls and petroleum pipelines. Studies indicated that there was an unusual amino acid 3,4-dihydroxy-l-phenylanine (dopa), which was the crucial super adhesive unit in the proteins. The technology of electrolyzing seawater was employed to generate HOCl solution to hinder the adhesion. However, the detailed anti-fouling mechanism of HOCl solution remained unknown to be fully explained. Herein, we theoretically reported a study of single molecular (dopa) reaction under the HOCl solution environment, which would be helpful to reveal the anti-fouling mechanism through electrolyzing seawater. By using the density functional theory (DFT) quantum mechanics procedure, we theoretically studied the reaction mechanism of the adhesive unit dopa in mussel with electrolyzing seawater. Two possible pathways (1 and 2) were obtained (Fig. 6). The transition state for each pathway was determined, the intrinsic reaction coordinate (IRC) was analyzed and the mechanism had been confirmed. The calculations indicated dopa tended to have electrophonic attacking substitution reaction to generate 3-chlorine-4,5-dihydroxyphenylalanine (dopa-Cl) with different pathways, which hindered the formulation of conjuncted dopa–dopa and thus the stickiness among mussel adhesive proteins reduced. The transition states computation showed that pathway (1) had one transition state (TS1-1) with an activation energy of 102.22 kJ mol−1, while pathway (2) had two transition states (TS2-1, TS2-2) with activation energies of 191.98 kJ mol−1 and 42.00 kJ mol−1 respectively and one intermediate (IM2-1). Rate constant value of pathway (1) was much bigger than that of pathway (2) regardless of high or low temperature, which meant that in the reaction process, pathway (1) was the favorable reaction step; but as the temperature rose, the competitiveness of pathway (2) gradually increased. After the theoretical calculation, we found that it was Cl+ played an important and direct role in the dopa's modification." @default.
- W2043284578 created "2016-06-24" @default.
- W2043284578 creator A5004312072 @default.
- W2043284578 creator A5018626623 @default.
- W2043284578 creator A5029821836 @default.
- W2043284578 creator A5070206807 @default.
- W2043284578 creator A5070571216 @default.
- W2043284578 creator A5080071652 @default.
- W2043284578 date "2009-05-01" @default.
- W2043284578 modified "2023-09-27" @default.
- W2043284578 title "Theoretical investigation on the reaction of adhesion unit dopa in mussel with electrolyzing seawater" @default.
- W2043284578 cites W1517513338 @default.
- W2043284578 cites W1964817163 @default.
- W2043284578 cites W1965752441 @default.
- W2043284578 cites W1966750682 @default.
- W2043284578 cites W1978365214 @default.
- W2043284578 cites W1983152536 @default.
- W2043284578 cites W1985583109 @default.
- W2043284578 cites W1991997404 @default.
- W2043284578 cites W2001154641 @default.
- W2043284578 cites W2006167320 @default.
- W2043284578 cites W2006765534 @default.
- W2043284578 cites W2011121154 @default.
- W2043284578 cites W2014436232 @default.
- W2043284578 cites W2023271753 @default.
- W2043284578 cites W2030976617 @default.
- W2043284578 cites W2058254489 @default.
- W2043284578 cites W2058985738 @default.
- W2043284578 cites W2086697233 @default.
- W2043284578 cites W2092244272 @default.
- W2043284578 cites W2093241258 @default.
- W2043284578 cites W2094620274 @default.
- W2043284578 cites W2102031778 @default.
- W2043284578 cites W2160738948 @default.
- W2043284578 cites W2169484878 @default.
- W2043284578 cites W2312434703 @default.
- W2043284578 cites W2951672535 @default.
- W2043284578 doi "https://doi.org/10.1016/j.colsurfb.2008.12.033" @default.
- W2043284578 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19185470" @default.
- W2043284578 hasPublicationYear "2009" @default.
- W2043284578 type Work @default.
- W2043284578 sameAs 2043284578 @default.
- W2043284578 citedByCount "12" @default.
- W2043284578 countsByYear W20432845782012 @default.
- W2043284578 countsByYear W20432845782014 @default.
- W2043284578 countsByYear W20432845782015 @default.
- W2043284578 countsByYear W20432845782017 @default.
- W2043284578 countsByYear W20432845782019 @default.
- W2043284578 countsByYear W20432845782022 @default.
- W2043284578 crossrefType "journal-article" @default.
- W2043284578 hasAuthorship W2043284578A5004312072 @default.
- W2043284578 hasAuthorship W2043284578A5018626623 @default.
- W2043284578 hasAuthorship W2043284578A5029821836 @default.
- W2043284578 hasAuthorship W2043284578A5070206807 @default.
- W2043284578 hasAuthorship W2043284578A5070571216 @default.
- W2043284578 hasAuthorship W2043284578A5080071652 @default.
- W2043284578 hasConcept C111368507 @default.
- W2043284578 hasConcept C115792997 @default.
- W2043284578 hasConcept C127313418 @default.
- W2043284578 hasConcept C147597530 @default.
- W2043284578 hasConcept C147789679 @default.
- W2043284578 hasConcept C161790260 @default.
- W2043284578 hasConcept C178790620 @default.
- W2043284578 hasConcept C185592680 @default.
- W2043284578 hasConcept C18903297 @default.
- W2043284578 hasConcept C197248824 @default.
- W2043284578 hasConcept C2779987062 @default.
- W2043284578 hasConcept C41625074 @default.
- W2043284578 hasConcept C55493867 @default.
- W2043284578 hasConcept C84416704 @default.
- W2043284578 hasConcept C86803240 @default.
- W2043284578 hasConcept C89031862 @default.
- W2043284578 hasConcept C95121573 @default.
- W2043284578 hasConceptScore W2043284578C111368507 @default.
- W2043284578 hasConceptScore W2043284578C115792997 @default.
- W2043284578 hasConceptScore W2043284578C127313418 @default.
- W2043284578 hasConceptScore W2043284578C147597530 @default.
- W2043284578 hasConceptScore W2043284578C147789679 @default.
- W2043284578 hasConceptScore W2043284578C161790260 @default.
- W2043284578 hasConceptScore W2043284578C178790620 @default.
- W2043284578 hasConceptScore W2043284578C185592680 @default.
- W2043284578 hasConceptScore W2043284578C18903297 @default.
- W2043284578 hasConceptScore W2043284578C197248824 @default.
- W2043284578 hasConceptScore W2043284578C2779987062 @default.
- W2043284578 hasConceptScore W2043284578C41625074 @default.
- W2043284578 hasConceptScore W2043284578C55493867 @default.
- W2043284578 hasConceptScore W2043284578C84416704 @default.
- W2043284578 hasConceptScore W2043284578C86803240 @default.
- W2043284578 hasConceptScore W2043284578C89031862 @default.
- W2043284578 hasConceptScore W2043284578C95121573 @default.
- W2043284578 hasIssue "2" @default.
- W2043284578 hasLocation W20432845781 @default.
- W2043284578 hasLocation W20432845782 @default.
- W2043284578 hasOpenAccess W2043284578 @default.
- W2043284578 hasPrimaryLocation W20432845781 @default.
- W2043284578 hasRelatedWork W1813305405 @default.
- W2043284578 hasRelatedWork W2048597607 @default.
- W2043284578 hasRelatedWork W2052108213 @default.