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Volumn 35, Issue 12, 1996, Pages 3702-3705

X-Band ENDOR of the Liganding Environment from the Radical X Intermediate of Escherichia coli Ribonucleotide Reductase

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Indexed keywords


EID: 0000753986     PISSN: 00201669     EISSN: None     Source Type: Journal    
DOI: 10.1021/ic951544i     Document Type: Article
Times cited : (18)

References (28)
  • 21
    • 85085666140 scopus 로고    scopus 로고
    • note
    • Fe(III). The upshot is that if intrinsic hyperfine tensors for nitrogen or protons are similar for Intermediate X, mixedvalent MMO, or semimet Hr, then the effective tensors and ENDOR frequencies also are similar.
  • 23
    • 2542548157 scopus 로고    scopus 로고
    • note
    • (III)2 were included in computing the tensor and there was no contribution from spin on the bridging oxygen, then the resultant rhombic dipolar tensor had principal values of 17.6, -21.9, and 4.3 MHz. In either case the two larger tensor values were ∼20 MHz in magnitude and were in the Fe-O-Fe plane,
  • 27
    • 0000389187 scopus 로고
    • Metalloenzyme Active Site Structure and Function by Multifrequency CW and Pulsed Electron Nuclear Double Resonance (ENDOR)
    • Berliner, L. J., Reuben, J., Eds.; Plenum Press: New York, Chapter 4
    • Hoffman, B. M.; DeRose, V. J.; Doan, P. E.; Gurbiel, R. J.; Housman, A. L. P.; Telser, J. Metalloenzyme Active Site Structure and Function by Multifrequency CW and Pulsed Electron Nuclear Double Resonance (ENDOR). In EMR of Paramagnetic Molecules; Biological Magnetic Resonance 13; Berliner, L. J., Reuben, J., Eds.; Plenum Press: New York, 1993; Chapter 4, pp 151-218.
    • (1993) EMR of Paramagnetic Molecules; Biological Magnetic Resonance , vol.13 , pp. 151-218
    • Hoffman, B.M.1    Derose, V.J.2    Doan, P.E.3    Gurbiel, R.J.4    Housman, A.L.P.5    Telser, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.