FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2011537598> ?p ?o ?g. }

• W2011537598 endingPage "6667" @default.
• W2011537598 startingPage "6659" @default.
• W2011537598 abstract "Although known to be important factors in promoting catalysis, electric field effects in enzyme active sites are difficult to characterize from an experimental standpoint. Among optical probes of electric fields, Raman spectroscopy has the advantage of being able to distinguish electronic ground-state and excited-state effects. Earlier Raman studies on acyl derivatives of cysteine proteases [Doran, J. D., and Carey, P. R. (1996) Biochemistry 35, 12495-502], where the acyl group has extensive pi-electron conjugation, showed that electric field effects in the active site manifest themselves by polarizing the pi-electrons of the acyl group. Polarization gives rise to large shifts in certain Raman bands, e.g. , the C=C stretching band of the alpha,beta-unsaturated acyl group, and a large red shift in the absorption maximum. It was postulated that a major source of polarization is the alpha-helix dipole that originates from the alpha-helix terminating at the active-site cysteine of the cysteine protease family. In contrast, using the acyl group 5-methylthiophene acryloyl (5-MTA) as an active-site Raman probe, acyl enzymes of thiol- or selenol-subtilisin exhibit no polarization even though the acylating amino acid is at the terminus of an alpha-helix. Quantum mechanical calculations on 5-MTA ethyl thiol and selenol ethyl esters allowed us to identify the conformational states of these molecules along with their corresponding vibrational signatures. The Raman spectra of 5-MTA thiol and selenol subtilisins both showed that the acyl group binds in a single conformation in the active site that is s-trans about the =C-C=O single bond. Moreover, the positions of the C=C stretching bands show that the acyl group is not experiencing polarization. However, the release of steric constraints in the active site by mutagenesis, by creating the N155G form of selenol-subtilisin and the P225A form of thiol-subtilisin, results in the appearance of a second conformer in the active sites that is s-cis about the =C-C=O bond. The Raman signature of this second conformer indicates that it is strongly polarized with a permanent dipole being set up through the acyl group's pi-electron chain. Molecular modeling for 5-MTA in the active sites of selenol-subtilisin and N155G selenol-subtilisin confirms the findings from Raman spectroscopic studies and identifies the active-site features that give rise to polarization. The determinants of polarization appear to be strong electron pull at the acyl carbonyl group by a combination of hydrogen bonds and the field at the N-terminus of the alpha-helix and electron push from a negatively charged group placed at the opposite end of the chromophore." @default.
• W2011537598 created "2016-06-24" @default.
• W2011537598 creator A5018207289 @default.
• W2011537598 creator A5031081898 @default.
• W2011537598 creator A5031224600 @default.
• W2011537598 creator A5044029247 @default.
• W2011537598 creator A5078465044 @default.
• W2011537598 creator A5082945130 @default.
• W2011537598 date "1999-04-30" @default.
• W2011537598 modified "2023-10-03" @default.
• W2011537598 title "Electric Fields in Active Sites: Substrate Switching from Null to Strong Fields in Thiol- and Selenol-Subtilisins" @default.
• W2011537598 cites W1883093314 @default.
• W2011537598 cites W1971022925 @default.
• W2011537598 cites W1996512279 @default.
• W2011537598 cites W2000772583 @default.
• W2011537598 cites W2038836954 @default.
• W2011537598 cites W2059428626 @default.
• W2011537598 cites W2059435270 @default.
• W2011537598 cites W2070785063 @default.
• W2011537598 cites W2081661375 @default.
• W2011537598 cites W2091097441 @default.
• W2011537598 cites W2108453057 @default.
• W2011537598 cites W2121096033 @default.
• W2011537598 cites W2322687521 @default.
• W2011537598 cites W2833117375 @default.
• W2011537598 doi "https://doi.org/10.1021/bi9902541" @default.
• W2011537598 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10350485" @default.
• W2011537598 hasPublicationYear "1999" @default.
• W2011537598 type Work @default.
• W2011537598 sameAs 2011537598 @default.
• W2011537598 citedByCount "12" @default.
• W2011537598 countsByYear W20115375982017 @default.
• W2011537598 crossrefType "journal-article" @default.
• W2011537598 hasAuthorship W2011537598A5018207289 @default.
• W2011537598 hasAuthorship W2011537598A5031081898 @default.
• W2011537598 hasAuthorship W2011537598A5031224600 @default.
• W2011537598 hasAuthorship W2011537598A5044029247 @default.
• W2011537598 hasAuthorship W2011537598A5078465044 @default.
• W2011537598 hasAuthorship W2011537598A5082945130 @default.
• W2011537598 hasConcept C120665830 @default.
• W2011537598 hasConcept C121332964 @default.
• W2011537598 hasConcept C161790260 @default.
• W2011537598 hasConcept C178790620 @default.
• W2011537598 hasConcept C181199279 @default.
• W2011537598 hasConcept C185592680 @default.
• W2011537598 hasConcept C193557335 @default.
• W2011537598 hasConcept C2779201268 @default.
• W2011537598 hasConcept C2781324293 @default.
• W2011537598 hasConcept C40003534 @default.
• W2011537598 hasConcept C41183919 @default.
• W2011537598 hasConcept C71240020 @default.
• W2011537598 hasConceptScore W2011537598C120665830 @default.
• W2011537598 hasConceptScore W2011537598C121332964 @default.
• W2011537598 hasConceptScore W2011537598C161790260 @default.
• W2011537598 hasConceptScore W2011537598C178790620 @default.
• W2011537598 hasConceptScore W2011537598C181199279 @default.
• W2011537598 hasConceptScore W2011537598C185592680 @default.
• W2011537598 hasConceptScore W2011537598C193557335 @default.
• W2011537598 hasConceptScore W2011537598C2779201268 @default.
• W2011537598 hasConceptScore W2011537598C2781324293 @default.
• W2011537598 hasConceptScore W2011537598C40003534 @default.
• W2011537598 hasConceptScore W2011537598C41183919 @default.
• W2011537598 hasConceptScore W2011537598C71240020 @default.
• W2011537598 hasIssue "20" @default.
• W2011537598 hasLocation W20115375981 @default.
• W2011537598 hasLocation W20115375982 @default.
• W2011537598 hasOpenAccess W2011537598 @default.
• W2011537598 hasPrimaryLocation W20115375981 @default.
• W2011537598 hasRelatedWork W1965996338 @default.
• W2011537598 hasRelatedWork W1999101999 @default.
• W2011537598 hasRelatedWork W2021006666 @default.
• W2011537598 hasRelatedWork W2046163248 @default.
• W2011537598 hasRelatedWork W2054217906 @default.
• W2011537598 hasRelatedWork W2058726456 @default.
• W2011537598 hasRelatedWork W2076844462 @default.
• W2011537598 hasRelatedWork W2198228037 @default.
• W2011537598 hasRelatedWork W2953155228 @default.
• W2011537598 hasRelatedWork W3203388139 @default.
• W2011537598 hasVolume "38" @default.
• W2011537598 isParatext "false" @default.
• W2011537598 isRetracted "false" @default.
• W2011537598 magId "2011537598" @default.
• W2011537598 workType "article" @default.