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Volumn 129, Issue 48, 2007, Pages 15060-15071

Site-specific insertion of 3-aminotyrosine into subunit α2 of E. coli ribonucleotide reductase: Direct evidence for involvement of Y730 and Y731 in radical propagation

Author keywords

[No Author keywords available]

Indexed keywords

3-AMINOTYROSINE; DEOXYNUCLEOTIDES; HYDROGEN ATOM TRANSFER MECHANISM;

EID: 36849004028     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja076043y     Document Type: Article
Times cited : (117)

References (97)
  • 62
    • 36849072050 scopus 로고
    • Ph.D. Thesis. Massachusetts Institute of Technology Cambridge, MA
    • Salowe, S. P. Ph.D. Thesis. Massachusetts Institute of Technology Cambridge, MA, 1992.
    • (1992)
    • Salowe, S.P.1
  • 79
    • 36848999948 scopus 로고    scopus 로고
    • A more detailed analysis of the new radical species will be presented elsewhere
    • A more detailed analysis of the new radical species will be presented elsewhere.
  • 84
    • 36849027765 scopus 로고    scopus 로고
    • Rapid chemical quench studies monitoring dCDP formation with intein-generated wt β2 no longer show a burst of dCDP formation (as with wt β2) but exhibit a single rate constant of ∼1 s_1 M. Seyedsayamdost, J. Stubbe, unpublished results, Thus, the slow phase observed with DOPA-β2 could also be kinetically competent in turnover
    • _1 (M. Seyedsayamdost, J. Stubbe, unpublished results). Thus, the slow phase observed with DOPA-β2 could also be kinetically competent in turnover.
  • 91
    • 36849023216 scopus 로고    scopus 로고
    • Previous computational studies on o-aminophenol have shown that the BDE of the phenolic hydroxyl group is lower than that of the amine. EPR studies on o-aminophenol are in line with these calculations demonstrating the presence of two N-bound protons in the oxidized state (see refs 90 and 96). Our own preliminary EPR simulations and DFT calculations also suggest that the structure of the radical is that shown in Scheme 1 (M. Seyedsayamdost, M. Bennati, J. Stubbe, unpublished results).
    • Previous computational studies on o-aminophenol have shown that the BDE of the phenolic hydroxyl group is lower than that of the amine. EPR studies on o-aminophenol are in line with these calculations demonstrating the presence of two N-bound protons in the oxidized state (see refs 90 and 96). Our own preliminary EPR simulations and DFT calculations also suggest that the structure of the radical is that shown in Scheme 1 (M. Seyedsayamdost, M. Bennati, J. Stubbe, unpublished results).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.