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Volumn 45, Issue 28, 2006, Pages 4546-4550

The first crystal structure of tyrosinase: All questions answered?

Author keywords

Bioinorganic chemistry; Copper; Metalloenzymes; Protein structures; Tyrosinase

Indexed keywords

BIOINORGANIC CHEMISTRY; METALLOENZYMES; PROTEIN STRUCTURES; TYROSINASE;

EID: 33746291588     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200601255     Document Type: Review
Times cited : (296)

References (32)
  • 15
    • 0037683397 scopus 로고    scopus 로고
    • (Eds.: A. Messerschmidt, R. Huber, T. Poulos, K. Wieghardt), Wiley, New York
    • C. Eicken, C. Gerdemann, B. Krebs, Handbook of Metalloproteins, Vol. 2 (Eds.: A. Messerschmidt, R. Huber, T. Poulos, K. Wieghardt), Wiley, New York, 2001, p. 1319.
    • (2001) Handbook of Metalloproteins, Vol. 2 , vol.2 , pp. 1319
    • Eicken, C.1    Gerdemann, C.2    Krebs, B.3
  • 30
    • 33746286213 scopus 로고    scopus 로고
    • note
    • The assignment of Matoba et al. is only correct for the deoxy and metI forms, which are not relevant for catalysis.
  • 31
    • 33746286497 scopus 로고    scopus 로고
    • note
    • 2, the differences in bond lengths are less distinct, but the Cu-N(His63) bond length is still the longest (2.20 vs. 2.19 and 2.14 Å). In the oxy form that is generated in the presence of dithiotreitol, the CuA-N(His63) bond is again much longer than the other ones (2.37 vs. 2.15 and 2.08 Å).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.