FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2076247612> ?p ?o ?g. }

• W2076247612 endingPage "2969" @default.
• W2076247612 startingPage "2961" @default.
• W2076247612 abstract "The coordination environments of two distinct metal sites on the bacterial photosynthetic reaction center (RC) protein were probed with pulsed electron paramagnetic resonance (EPR) spectroscopy. For these studies, Cu2+ was bound specifically to a surface site on native Fe2+-containing RCs from Rhodobacter sphaeroides R-26 and to the native non-heme Fe site in biochemically Fe-removed RCs. The cw and pulsed EPR results clearly indicate two spectroscopically different Cu2+ environments. In the dark, the RCs with Cu2+ bound to the surface site exhibit an axially symmetric EPR spectrum with g(parallel) = 2.24, A(parallel) = 160 G, g(perpendicular) = 2.06, whereas the values g(parallel) = 2.31, A(parallel) = 143 G, and g(perpendicular) = 2.07 were observed when Cu(2+) was substituted in the Fe site. Examination of the light-induced spectral changes indicate that the surface Cu2+ is at least 23 A removed from the primary donor (P+) and reduced quinone acceptor (QA-). Electron spin-echo envelope modulation (ESEEM) spectra of these Cu-RC proteins have been obtained and provide the first direct solution structural information about the ligands in the surface metal site. From these pulsed EPR experiments, modulations were observed that are consistent with multiple weakly hyperfine coupled 14N nuclei in close proximity to Cu2+, indicating that two or more histidines ligate the Cu2+ at the surface site. Thus, metal and EPR analyses confirm that we have developed reliable methods for stoichiometrically and specifically binding Cu2+ to a surface site that is distinct from the well characterized Fe site and support the view that Cu2+ is bound at or near the Zn site that modulates electron transfer between the quinones QA and QB (QA-QB --> QAQB-) (Utschig, L. M., Ohigashi, Y., Thurnauer, M. C., and Tiede, D. M (1998) Biochemistry 37, 8278-8281) and proton uptake by QB- (Paddock, M. L., Graige, M. S., Feher, G., and Okamura, M. Y. (1999) Proc. Natl. Acad. Sci. U.S.A. 96, 6183-6188). Detailed EPR spectroscopic characterization of these Cu2+-RCs will provide a means to investigate the role of local protein environments in modulating electron and proton transfer." @default.
• W2076247612 created "2016-06-24" @default.
• W2076247612 creator A5005892636 @default.
• W2076247612 creator A5014669390 @default.
• W2076247612 creator A5067725076 @default.
• W2076247612 creator A5081322051 @default.
• W2076247612 date "2000-02-26" @default.
• W2076247612 modified "2023-10-14" @default.
• W2076247612 title "EPR Investigation of Cu²⁺-Substituted Photosynthetic Bacterial Reaction Centers: Evidence for Histidine Ligation at the Surface Metal Site" @default.
• W2076247612 cites W1537270003 @default.
• W2076247612 cites W162335599 @default.
• W2076247612 cites W1994800007 @default.
• W2076247612 cites W2001866541 @default.
• W2076247612 cites W2019897361 @default.
• W2076247612 cites W2035603915 @default.
• W2076247612 cites W2043004601 @default.
• W2076247612 cites W2048645097 @default.
• W2076247612 cites W2077535029 @default.
• W2076247612 cites W2077683669 @default.
• W2076247612 cites W2090314541 @default.
• W2076247612 cites W2091198557 @default.
• W2076247612 cites W2092922885 @default.
• W2076247612 cites W4240709567 @default.
• W2076247612 doi "https://doi.org/10.1021/bi991800t" @default.
• W2076247612 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10715116" @default.
• W2076247612 hasPublicationYear "2000" @default.
• W2076247612 type Work @default.
• W2076247612 sameAs 2076247612 @default.
• W2076247612 citedByCount "25" @default.
• W2076247612 countsByYear W20762476122012 @default.
• W2076247612 countsByYear W20762476122013 @default.
• W2076247612 countsByYear W20762476122014 @default.
• W2076247612 countsByYear W20762476122019 @default.
• W2076247612 crossrefType "journal-article" @default.
• W2076247612 hasAuthorship W2076247612A5005892636 @default.
• W2076247612 hasAuthorship W2076247612A5014669390 @default.
• W2076247612 hasAuthorship W2076247612A5067725076 @default.
• W2076247612 hasAuthorship W2076247612A5081322051 @default.
• W2076247612 hasConcept C121332964 @default.
• W2076247612 hasConcept C123669783 @default.
• W2076247612 hasConcept C126838900 @default.
• W2076247612 hasConcept C131538251 @default.
• W2076247612 hasConcept C143409427 @default.
• W2076247612 hasConcept C177462420 @default.
• W2076247612 hasConcept C178790620 @default.
• W2076247612 hasConcept C183688256 @default.
• W2076247612 hasConcept C184779094 @default.
• W2076247612 hasConcept C185592680 @default.
• W2076247612 hasConcept C187961010 @default.
• W2076247612 hasConcept C188231169 @default.
• W2076247612 hasConcept C193812863 @default.
• W2076247612 hasConcept C2777897970 @default.
• W2076247612 hasConcept C46141821 @default.
• W2076247612 hasConcept C544153396 @default.
• W2076247612 hasConcept C55493867 @default.
• W2076247612 hasConcept C71924100 @default.
• W2076247612 hasConcept C75473681 @default.
• W2076247612 hasConcept C8010536 @default.
• W2076247612 hasConcept C83042744 @default.
• W2076247612 hasConceptScore W2076247612C121332964 @default.
• W2076247612 hasConceptScore W2076247612C123669783 @default.
• W2076247612 hasConceptScore W2076247612C126838900 @default.
• W2076247612 hasConceptScore W2076247612C131538251 @default.
• W2076247612 hasConceptScore W2076247612C143409427 @default.
• W2076247612 hasConceptScore W2076247612C177462420 @default.
• W2076247612 hasConceptScore W2076247612C178790620 @default.
• W2076247612 hasConceptScore W2076247612C183688256 @default.
• W2076247612 hasConceptScore W2076247612C184779094 @default.
• W2076247612 hasConceptScore W2076247612C185592680 @default.
• W2076247612 hasConceptScore W2076247612C187961010 @default.
• W2076247612 hasConceptScore W2076247612C188231169 @default.
• W2076247612 hasConceptScore W2076247612C193812863 @default.
• W2076247612 hasConceptScore W2076247612C2777897970 @default.
• W2076247612 hasConceptScore W2076247612C46141821 @default.
• W2076247612 hasConceptScore W2076247612C544153396 @default.
• W2076247612 hasConceptScore W2076247612C55493867 @default.
• W2076247612 hasConceptScore W2076247612C71924100 @default.
• W2076247612 hasConceptScore W2076247612C75473681 @default.
• W2076247612 hasConceptScore W2076247612C8010536 @default.
• W2076247612 hasConceptScore W2076247612C83042744 @default.
• W2076247612 hasIssue "11" @default.
• W2076247612 hasLocation W20762476121 @default.
• W2076247612 hasLocation W20762476122 @default.
• W2076247612 hasOpenAccess W2076247612 @default.
• W2076247612 hasPrimaryLocation W20762476121 @default.
• W2076247612 hasRelatedWork W182520765 @default.
• W2076247612 hasRelatedWork W1966429303 @default.
• W2076247612 hasRelatedWork W1978023710 @default.
• W2076247612 hasRelatedWork W1997279160 @default.
• W2076247612 hasRelatedWork W2006796120 @default.
• W2076247612 hasRelatedWork W2036243783 @default.
• W2076247612 hasRelatedWork W2046216903 @default.
• W2076247612 hasRelatedWork W2076247612 @default.
• W2076247612 hasRelatedWork W2077683669 @default.
• W2076247612 hasRelatedWork W2740625920 @default.
• W2076247612 hasVolume "39" @default.
• W2076247612 isParatext "false" @default.
• W2076247612 isRetracted "false" @default.

• next