FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2023186717> ?p ?o ?g. }

• W2023186717 endingPage "9850" @default.
• W2023186717 startingPage "9845" @default.
• W2023186717 abstract "The mutant form Phe-208-->Tyr of the R2 protein of Escherichia coli ribonucleotide reductase contains an intrinsic ferric-Dopa cofactor with characteristic absorption bands at 460 and ca. 700 nm [Ormö, M., de Maré, F., Regnström, K., Aberg, A., Sahlin, M., Ling, J., Loehr, T. M., Sanders-Loehr, J., & Sjöberg, B. M. (1992) J. Biol. Chem. 267, 8711-8714]. The three-dimensional structure of the mutant protein, solved to 2.5-A resolution, shows that the Dopa is localized to residue 208 and that it is a bidentate ligand of Fe1 of the binuclear iron center of protein R2. Nascent apoR2 F208Y, lacking metal ions, can be purified from overproducing cells grown in iron-depleted medium. ApoR2 F208Y is rapidly and quantitatively converted to the Dopa-208 form in vitro by addition of ferrous iron in the presence of oxygen. Other metal ions (Cu2+, Mn2+, Co2+) known to bind to the metal site of wild-type apoR2 do not generate a Dopa in apoR2 F208Y. The autocatalytic generation of Dopa does not require the presence of a tyrosine residue at position 122, the tyrosine which in a wild-type R2 protein acquires the catalytically essential tyrosyl radical. It is proposed that generation of Dopa initially follows the suggested reaction mechanism for tyrosyl radical generation in the wild-type protein and involves a ferryl intermediate, which in the case of the mutant R2 protein oxygenates Tyr 208. This autocatalytic metal-mediated reaction in the engineered R2 F208Y protein may serve as a model for formation of covalently bound quinones in other proteins." @default.
• W2023186717 created "2016-06-24" @default.
• W2023186717 creator A5003281486 @default.
• W2023186717 creator A5037548184 @default.
• W2023186717 creator A5060431795 @default.
• W2023186717 creator A5075967631 @default.
• W2023186717 date "1993-09-21" @default.
• W2023186717 modified "2023-10-17" @default.
• W2023186717 title "Autocatalytic generation of Dopa in the engineered protein R2 F208Y from Escherichia coli ribonucleotide reductase and crystal structure of the Dopa-208 protein" @default.
• W2023186717 cites W105526937 @default.
• W2023186717 cites W106612973 @default.
• W2023186717 cites W1510103500 @default.
• W2023186717 cites W1544469036 @default.
• W2023186717 cites W1550250656 @default.
• W2023186717 cites W1575785934 @default.
• W2023186717 cites W1603488046 @default.
• W2023186717 cites W1644644959 @default.
• W2023186717 cites W185850242 @default.
• W2023186717 cites W1970220520 @default.
• W2023186717 cites W1971321994 @default.
• W2023186717 cites W1975914851 @default.
• W2023186717 cites W1998673090 @default.
• W2023186717 cites W2010105734 @default.
• W2023186717 cites W2010785482 @default.
• W2023186717 cites W2024610281 @default.
• W2023186717 cites W2034802577 @default.
• W2023186717 cites W2045455413 @default.
• W2023186717 cites W2068518785 @default.
• W2023186717 cites W2069350944 @default.
• W2023186717 cites W2071707784 @default.
• W2023186717 cites W2091573044 @default.
• W2023186717 cites W2125833878 @default.
• W2023186717 cites W2145442226 @default.
• W2023186717 doi "https://doi.org/10.1021/bi00088a040" @default.
• W2023186717 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8373782" @default.
• W2023186717 hasPublicationYear "1993" @default.
• W2023186717 type Work @default.
• W2023186717 sameAs 2023186717 @default.
• W2023186717 citedByCount "54" @default.
• W2023186717 countsByYear W20231867172012 @default.
• W2023186717 countsByYear W20231867172015 @default.
• W2023186717 countsByYear W20231867172018 @default.
• W2023186717 crossrefType "journal-article" @default.
• W2023186717 hasAuthorship W2023186717A5003281486 @default.
• W2023186717 hasAuthorship W2023186717A5037548184 @default.
• W2023186717 hasAuthorship W2023186717A5060431795 @default.
• W2023186717 hasAuthorship W2023186717A5075967631 @default.
• W2023186717 hasConcept C104292427 @default.
• W2023186717 hasConcept C104317684 @default.
• W2023186717 hasConcept C143065580 @default.
• W2023186717 hasConcept C161790260 @default.
• W2023186717 hasConcept C178790620 @default.
• W2023186717 hasConcept C181199279 @default.
• W2023186717 hasConcept C185592680 @default.
• W2023186717 hasConcept C197957613 @default.
• W2023186717 hasConcept C207583985 @default.
• W2023186717 hasConcept C2775832776 @default.
• W2023186717 hasConcept C2776165026 @default.
• W2023186717 hasConcept C2781338088 @default.
• W2023186717 hasConcept C37263863 @default.
• W2023186717 hasConcept C4710235 @default.
• W2023186717 hasConcept C547475151 @default.
• W2023186717 hasConcept C55493867 @default.
• W2023186717 hasConcept C71240020 @default.
• W2023186717 hasConceptScore W2023186717C104292427 @default.
• W2023186717 hasConceptScore W2023186717C104317684 @default.
• W2023186717 hasConceptScore W2023186717C143065580 @default.
• W2023186717 hasConceptScore W2023186717C161790260 @default.
• W2023186717 hasConceptScore W2023186717C178790620 @default.
• W2023186717 hasConceptScore W2023186717C181199279 @default.
• W2023186717 hasConceptScore W2023186717C185592680 @default.
• W2023186717 hasConceptScore W2023186717C197957613 @default.
• W2023186717 hasConceptScore W2023186717C207583985 @default.
• W2023186717 hasConceptScore W2023186717C2775832776 @default.
• W2023186717 hasConceptScore W2023186717C2776165026 @default.
• W2023186717 hasConceptScore W2023186717C2781338088 @default.
• W2023186717 hasConceptScore W2023186717C37263863 @default.
• W2023186717 hasConceptScore W2023186717C4710235 @default.
• W2023186717 hasConceptScore W2023186717C547475151 @default.
• W2023186717 hasConceptScore W2023186717C55493867 @default.
• W2023186717 hasConceptScore W2023186717C71240020 @default.
• W2023186717 hasIssue "37" @default.
• W2023186717 hasLocation W20231867171 @default.
• W2023186717 hasLocation W20231867172 @default.
• W2023186717 hasOpenAccess W2023186717 @default.
• W2023186717 hasPrimaryLocation W20231867171 @default.
• W2023186717 hasRelatedWork W1481018570 @default.
• W2023186717 hasRelatedWork W1508691356 @default.
• W2023186717 hasRelatedWork W1535449341 @default.
• W2023186717 hasRelatedWork W1981142562 @default.
• W2023186717 hasRelatedWork W2017748671 @default.
• W2023186717 hasRelatedWork W2026603700 @default.
• W2023186717 hasRelatedWork W2131990102 @default.
• W2023186717 hasRelatedWork W2412169582 @default.
• W2023186717 hasRelatedWork W3014578680 @default.
• W2023186717 hasRelatedWork W86974628 @default.
• W2023186717 hasVolume "32" @default.
• W2023186717 isParatext "false" @default.

• next