Matches in SemOpenAlex for { <https://semopenalex.org/work/W1616577586> ?p ?o ?g. }
Showing items 1 to 75 of
75
with 100 items per page.
- W1616577586 endingPage "6321" @default.
- W1616577586 startingPage "6317" @default.
- W1616577586 abstract "Photooxidation of Rhodobacter capsulatus cytochrome c2 and four site-directed mutants by detergent solubilized Rhodobacter sphaeroides reaction centers was studied as a function of ionic strength at pH 8.0. Mutants of cytochrome c2 included K12D (lysine 12 substituted by aspartate), K14E (lysine 14 substituted by glutamate), K32E (lysine 32 substituted by glutamate), and K14E/K32E (lysines 14 and 32 substituted by glutamates). With respect to the wild-type, the mutants exhibited decreased second-order rate constants, indicating perturbation of their electrostatic interaction with the reaction center. In the transient complex, the interaction domain charges of the reaction center and wild-type cytochrome c2 were estimated to be -4.8 and +4.8, respectively. In contrast, the interaction domain charges of mutants K12D, K14E, K32E, and K14E/K32E were estimated to be +2.8, +3.7, +3.6 and +1.3, respectively. At infinite ionic strength, the second-order rate constant of the wild-type cytochrome c2 photooxidation (k infinity) was estimated to be 8.7 x 10(6) M-1 s-1. In the case of K32E, k infinity was not changed significantly (8.2 x 10(6) m-1 s-1), suggesting that the electrostatic perturbation of this mutant was largely overcome at high ionic strength. In contrast, the k infinity for K12D, K14E, and K14E/K32E were estimated to be decreased 2-7-fold. Consequently, mutations to R. capsulatus lysines 12 and 14 appear to perturb the distance and/or orientation of the cytochrome c2 relative to the reaction center in the reactive complex, as well as alter electrostatic interactions. Based upon the kinetic results presented here, the cytochrome c2-reaction center transient complex has been modeled." @default.
- W1616577586 created "2016-06-24" @default.
- W1616577586 creator A5005253617 @default.
- W1616577586 creator A5019348558 @default.
- W1616577586 creator A5085664852 @default.
- W1616577586 date "1992-03-01" @default.
- W1616577586 modified "2023-10-03" @default.
- W1616577586 title "Study of the cytochrome c2-reaction center interaction by site-directed mutagenesis." @default.
- W1616577586 cites W1525091849 @default.
- W1616577586 cites W1538116895 @default.
- W1616577586 cites W1554077494 @default.
- W1616577586 cites W1645025205 @default.
- W1616577586 cites W1970312228 @default.
- W1616577586 cites W1988917178 @default.
- W1616577586 cites W2012041242 @default.
- W1616577586 cites W2015935520 @default.
- W1616577586 cites W2048800899 @default.
- W1616577586 cites W2049017963 @default.
- W1616577586 cites W2059235873 @default.
- W1616577586 cites W2061633149 @default.
- W1616577586 cites W2066823211 @default.
- W1616577586 cites W2071874978 @default.
- W1616577586 cites W2088604360 @default.
- W1616577586 cites W2092978809 @default.
- W1616577586 cites W2161779691 @default.
- W1616577586 cites W87003245 @default.
- W1616577586 cites W2007907670 @default.
- W1616577586 doi "https://doi.org/10.1016/s0021-9258(18)42698-1" @default.
- W1616577586 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1313433" @default.
- W1616577586 hasPublicationYear "1992" @default.
- W1616577586 type Work @default.
- W1616577586 sameAs 1616577586 @default.
- W1616577586 citedByCount "42" @default.
- W1616577586 crossrefType "journal-article" @default.
- W1616577586 hasAuthorship W1616577586A5005253617 @default.
- W1616577586 hasAuthorship W1616577586A5019348558 @default.
- W1616577586 hasAuthorship W1616577586A5085664852 @default.
- W1616577586 hasBestOaLocation W16165775861 @default.
- W1616577586 hasConcept C103408237 @default.
- W1616577586 hasConcept C104317684 @default.
- W1616577586 hasConcept C143065580 @default.
- W1616577586 hasConcept C16318435 @default.
- W1616577586 hasConcept C185592680 @default.
- W1616577586 hasConcept C501734568 @default.
- W1616577586 hasConcept C55493867 @default.
- W1616577586 hasConcept C71240020 @default.
- W1616577586 hasConceptScore W1616577586C103408237 @default.
- W1616577586 hasConceptScore W1616577586C104317684 @default.
- W1616577586 hasConceptScore W1616577586C143065580 @default.
- W1616577586 hasConceptScore W1616577586C16318435 @default.
- W1616577586 hasConceptScore W1616577586C185592680 @default.
- W1616577586 hasConceptScore W1616577586C501734568 @default.
- W1616577586 hasConceptScore W1616577586C55493867 @default.
- W1616577586 hasConceptScore W1616577586C71240020 @default.
- W1616577586 hasIssue "9" @default.
- W1616577586 hasLocation W16165775861 @default.
- W1616577586 hasOpenAccess W1616577586 @default.
- W1616577586 hasPrimaryLocation W16165775861 @default.
- W1616577586 hasRelatedWork W1572324330 @default.
- W1616577586 hasRelatedWork W2007231835 @default.
- W1616577586 hasRelatedWork W2024647076 @default.
- W1616577586 hasRelatedWork W2145441838 @default.
- W1616577586 hasRelatedWork W2358175167 @default.
- W1616577586 hasRelatedWork W2365402183 @default.
- W1616577586 hasRelatedWork W2528862892 @default.
- W1616577586 hasRelatedWork W2565847177 @default.
- W1616577586 hasRelatedWork W2587315940 @default.
- W1616577586 hasRelatedWork W4246966729 @default.
- W1616577586 hasVolume "267" @default.
- W1616577586 isParatext "false" @default.
- W1616577586 isRetracted "false" @default.
- W1616577586 magId "1616577586" @default.
- W1616577586 workType "article" @default.