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Volumn 121, Issue 11, 1999, Pages 2346-2352

The crystal structure of an azide complex of the diferrous R2 subunit of ribonucleotide reductase displays a novel carboxylate shift with important mechanistic implications for diiron-catalyzed oxygen activation

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A DESATURASE; AZIDE; CARBOXYLIC ACID; GLUTAMIC ACID; IRON; LIGAND; METHANE MONOOXYGENASE; MUTANT PROTEIN; OXYGEN; RIBONUCLEOTIDE REDUCTASE; TYROSINE;

EID: 0033599495     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja982280c     Document Type: Article
Times cited : (98)

References (62)
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    • Collaborative computational project, no. 4: Acta Crystallogr. C 1994, 50, 760-763.
    • (1994) Acta Crystallogr. C , vol.50 , pp. 760-763
  • 47
    • 0026597444 scopus 로고
    • Brünger, A. Nature 1992, 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.1
  • 53
    • 13044301672 scopus 로고    scopus 로고
    • 59,60. In the protein, steric effects would make it difficult to accommodate seven ligands to any of the Fe ions. Furthermore, seven-coordinate Fe ions have never been proposed to be involved in these reactions
    • 59,60. In the protein, steric effects would make it difficult to accommodate seven ligands to any of the Fe ions. Furthermore, seven-coordinate Fe ions have never been proposed to be involved in these reactions.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.