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Volumn 316, Issue 5823, 2007, Pages 453-457

Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates

Author keywords

[No Author keywords available]

Indexed keywords

3,4 DIHYDROXYPHENYLACETATE 2,3 DIOXYGENASE; 4 NITROCATECHOL; ALKYL GROUP; CARBOXYLIC ACID; DIOXYGENASE; FERROUS ION; HISTIDINE; OXYGEN; UNCLASSIFIED DRUG; 3,4-DIHYDROXYPHENYLACETATE 2,3-DIOXYGENASE; 4-NITROCATECHOL; CATECHOL DERIVATIVE; FERRIC ION; LIGAND; PROTEIN SUBUNIT; SUPEROXIDE;

EID: 34247534094     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1134697     Document Type: Article
Times cited : (319)

References (33)
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    • 34247529183 scopus 로고    scopus 로고
    • Visible residues out of a total of 365: C-terminal-deleted enzyme, 4-322 (PDB 1F1X); original full-length enzyme, 4-359 (PDB 1Q0O); Form reported here, 4-362 (PDB 2IG9, 2IGA).
    • Visible residues out of a total of 365: C-terminal-deleted enzyme, 4-322 (PDB 1F1X); original full-length enzyme, 4-359 (PDB 1Q0O); Form reported here, 4-362 (PDB 2IG9, 2IGA).
  • 15
    • 34247508332 scopus 로고    scopus 로고
    • Materials and methods and structure statistics (table 51) are available as supporting material on online
    • Materials and methods and structure statistics (table 51) are available as supporting material on Science online.
    • Science
  • 19
    • 34247550496 scopus 로고    scopus 로고
    • O2, where O1 is that which remains bound to the iron in the alkylperoxo intermediate.
    • O2, where O1 is that which remains bound to the iron in the alkylperoxo intermediate.
  • 20
    • 34247485130 scopus 로고    scopus 로고
    • 2 is present in the crystallization medium. Attempts to fit the electron density without a diatomic molecule, with only a single atom, or with two solvents were unsuccessful (fig. 54).
    • 2 is present in the crystallization medium. Attempts to fit the electron density without a diatomic molecule, with only a single atom, or with two solvents were unsuccessful (fig. 54).
  • 21
    • 34247506501 scopus 로고    scopus 로고
    • At the current resolution 1.95 Å, diatomic bond lengths between 1.2 and 1.4 Å could be used to fit the electron density. Thus, the state of reduction of the bound O2 could not be determined from the density alone
    • 2 could not be determined from the density alone.
  • 22
    • 34247546369 scopus 로고    scopus 로고
    • Although no appropriate model complex for an Fe2+ alkylperoxo species has been reported, a Mn(II) chelate complex exhibits an O-O bond length of 1.411 Å, similar to that of free H2O2 31
    • 2 (31).
  • 23
    • 34247539700 scopus 로고    scopus 로고
    • The electron density is low for the three carbons closest to the nitro substituent supporting the presence of the more flexible, ring-open product in the active site. Product from 4NC was soaked into a crystal of 2,3-HPCD, and it assumed the same structure fig. 52
    • The electron density is low for the three carbons closest to the nitro substituent supporting the presence of the more flexible, ring-open product in the active site. Product from 4NC was soaked into a crystal of 2,3-HPCD, and it assumed the same structure (fig. 52).
  • 26
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    • A. Karlsson et al., Science 299, 1039 (2003).
    • (2003) Science , vol.299 , pp. 1039
    • Karlsson, A.1
  • 32
    • 34247478752 scopus 로고    scopus 로고
    • Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
    • Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
  • 33
    • 34247524810 scopus 로고    scopus 로고
    • The authors thank A. R. Pearson, B. J. Johnson, C. M. Wilmot, and D. H. Ohlendorf for their guidance and critical discussions during the course of this work, and J. C. Nix for technical assistance in data collection. This work was supported by National Institute of General Medical Sciences GM246B9. We are grateful for beam time and assistance with x-ray data collection at the Lawrence Berkeley Laboratory Advanced Light Source (ALS, and for facilities and computer support from the Minnesota Supercomputing Institute. Coordinates have been deposited in the Protein Data Bank (PDB, as entries 2IG9 (full-length enzyme) and 2IGA enzyme reacted with 4NC and O2
    • 2).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.