Matches in SemOpenAlex for { <https://semopenalex.org/work/W1484289957> ?p ?o ?g. }
Showing items 1 to 84 of
84
with 100 items per page.
- W1484289957 endingPage "1965" @default.
- W1484289957 startingPage "1959" @default.
- W1484289957 abstract "The techniques of fluorescence enhancement, fluorescence quenching, fluorescence polarization, and equilibrium dialysis are utilized to study the binding properties of coenzyme to horse liver alcohol dehydrogenase. Polarization of fluorescence and equilibrium dialysis show that NADH binds to alcohol dehydrogenase with a stoichiometry of 6 mol per mol of enzyme, in contrast to the value of 2 determined from fluorescence enhancement measurements. NAD+ also binds with a stoichiometry of six as was determined by equilibrium dialysis. The two NADH sites which bind coenzyme more tightly and which are revealed by fluorescence enhancement measurements are designated the catalytic sites. Binding of coenzyme to the four ancillary sites does not alter the quantum yield of NADH but results in a 20% contribution to quenching of enzyme's tryptophan fluorescence. From the emission anisotropy of bound NADH of 24.0% for the additional sites and 28.1% for the catalytic sites and their relative fluorescence lifetimes at the same wavelengths of excitation and emmision, we conclude that the nicotinamide ring of NADH bound to the additional sites exhibits a freedom of motion independent of the macromolecule, while that bound to the catalytic sites is more rigidly held. Polarization of fluorescence yields negative intrinsic free energies of 9.2 and 7.5 Cal M-1 for NADH interaction with the catalytic and additional sites, respectively. Although these values are 1.3 to 2.0 Cal higher than those determined by fluorescence quenching and equilibrium dialysis, the mean Hill coefficient of 1.76 plus or minus 0.06, the titration span of 2.4 logarithmic units and coupling free energies (in magnitude and sign) are the same for all these techniques. The above difference in the intrinsic free energies are attributed largely to the different modes of interaction of excited and unexcited NADH molecules with alcohol dehydrogenase." @default.
- W1484289957 created "2016-06-24" @default.
- W1484289957 creator A5012958448 @default.
- W1484289957 creator A5049966641 @default.
- W1484289957 date "1975-03-01" @default.
- W1484289957 modified "2023-10-16" @default.
- W1484289957 title "Coenzyme interaction with horse liver alcohol dehydrogenase. Evidence for allosteric coenzyme binding sites from thermodynamic equilibrium studies." @default.
- W1484289957 cites W1256384604 @default.
- W1484289957 cites W1449826603 @default.
- W1484289957 cites W1539792476 @default.
- W1484289957 cites W1971240442 @default.
- W1484289957 cites W1986865163 @default.
- W1484289957 cites W1989371249 @default.
- W1484289957 cites W1991551431 @default.
- W1484289957 cites W1993814815 @default.
- W1484289957 cites W1996131560 @default.
- W1484289957 cites W2004718659 @default.
- W1484289957 cites W2008266112 @default.
- W1484289957 cites W2009652285 @default.
- W1484289957 cites W2010647915 @default.
- W1484289957 cites W2011305816 @default.
- W1484289957 cites W2013244604 @default.
- W1484289957 cites W2017773577 @default.
- W1484289957 cites W2024830970 @default.
- W1484289957 cites W2028945742 @default.
- W1484289957 cites W2068625312 @default.
- W1484289957 cites W2081517135 @default.
- W1484289957 cites W2090845969 @default.
- W1484289957 cites W2107051040 @default.
- W1484289957 cites W2159916641 @default.
- W1484289957 cites W2231483212 @default.
- W1484289957 cites W2413573908 @default.
- W1484289957 cites W3085207721 @default.
- W1484289957 doi "https://doi.org/10.1016/s0021-9258(19)41669-4" @default.
- W1484289957 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/163820" @default.
- W1484289957 hasPublicationYear "1975" @default.
- W1484289957 type Work @default.
- W1484289957 sameAs 1484289957 @default.
- W1484289957 citedByCount "11" @default.
- W1484289957 crossrefType "journal-article" @default.
- W1484289957 hasAuthorship W1484289957A5012958448 @default.
- W1484289957 hasAuthorship W1484289957A5049966641 @default.
- W1484289957 hasBestOaLocation W14842899571 @default.
- W1484289957 hasConcept C134651460 @default.
- W1484289957 hasConcept C166342909 @default.
- W1484289957 hasConcept C181199279 @default.
- W1484289957 hasConcept C185592680 @default.
- W1484289957 hasConcept C197957613 @default.
- W1484289957 hasConcept C2777344606 @default.
- W1484289957 hasConcept C2779123261 @default.
- W1484289957 hasConcept C2781415988 @default.
- W1484289957 hasConcept C55493867 @default.
- W1484289957 hasConcept C75520062 @default.
- W1484289957 hasConceptScore W1484289957C134651460 @default.
- W1484289957 hasConceptScore W1484289957C166342909 @default.
- W1484289957 hasConceptScore W1484289957C181199279 @default.
- W1484289957 hasConceptScore W1484289957C185592680 @default.
- W1484289957 hasConceptScore W1484289957C197957613 @default.
- W1484289957 hasConceptScore W1484289957C2777344606 @default.
- W1484289957 hasConceptScore W1484289957C2779123261 @default.
- W1484289957 hasConceptScore W1484289957C2781415988 @default.
- W1484289957 hasConceptScore W1484289957C55493867 @default.
- W1484289957 hasConceptScore W1484289957C75520062 @default.
- W1484289957 hasIssue "6" @default.
- W1484289957 hasLocation W14842899571 @default.
- W1484289957 hasOpenAccess W1484289957 @default.
- W1484289957 hasPrimaryLocation W14842899571 @default.
- W1484289957 hasRelatedWork W134642770 @default.
- W1484289957 hasRelatedWork W1484289957 @default.
- W1484289957 hasRelatedWork W1542448467 @default.
- W1484289957 hasRelatedWork W1797418561 @default.
- W1484289957 hasRelatedWork W1976949980 @default.
- W1484289957 hasRelatedWork W1997774441 @default.
- W1484289957 hasRelatedWork W1998304465 @default.
- W1484289957 hasRelatedWork W2137739899 @default.
- W1484289957 hasRelatedWork W2170874906 @default.
- W1484289957 hasRelatedWork W2330422603 @default.
- W1484289957 hasVolume "250" @default.
- W1484289957 isParatext "false" @default.
- W1484289957 isRetracted "false" @default.
- W1484289957 magId "1484289957" @default.
- W1484289957 workType "article" @default.