-
2
-
-
1542378704
-
-
M. Costas, M. P. Mehn, M. P. Jensen, L. Que Jr., Chem. Rev. 104, 939 (2004).
-
(2004)
Chem. Rev
, vol.104
, pp. 939
-
-
Costas, M.1
Mehn, M.P.2
Jensen, M.P.3
Que Jr., L.4
-
7
-
-
0036965765
-
-
N. Sato et al., J. Mol. Biol. 321, 621 (2002).
-
(2002)
J. Mol. Biol
, vol.321
, pp. 621
-
-
Sato, N.1
-
8
-
-
0029038688
-
-
L. Shu et al., Biochemistry 34, 6649 (1995).
-
(1995)
Biochemistry
, vol.34
, pp. 6649
-
-
Shu, L.1
-
9
-
-
0028862027
-
-
S. Han, L. D. Eltis, K. N. Timmis, S. W. Muchmore, J. T. Bolin, Science 270, 976 (1995).
-
(1995)
Science
, vol.270
, pp. 976
-
-
Han, S.1
Eltis, L.D.2
Timmis, K.N.3
Muchmore, S.W.4
Bolin, J.T.5
-
10
-
-
1642264726
-
-
M. W. Vetting, L. P. Wackett, L. Que Jr., J. D. Lipscomb, D. H. Ohlendorf, J. Bacteriol. 186, 1945 (2004).
-
(2004)
J. Bacteriol
, vol.186
, pp. 1945
-
-
Vetting, M.W.1
Wackett, L.P.2
Que Jr., L.3
Lipscomb, J.D.4
Ohlendorf, D.H.5
-
14
-
-
34247529183
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
0347264753
-
-
A. Karlsson et al., Science 299, 1039 (2003).
-
(2003)
Science
, vol.299
, pp. 1039
-
-
Karlsson, A.1
-
27
-
-
0035910409
-
-
M. D. Wolfe, J. V. Parales, D. T. Gibson, J. D. Lipscomb, J. Biol. Chem. 276, 1945 (2001).
-
(2001)
J. Biol. Chem
, vol.276
, pp. 1945
-
-
Wolfe, M.D.1
Parales, J.V.2
Gibson, D.T.3
Lipscomb, J.D.4
-
32
-
-
34247478752
-
-
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
-
-
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).
-
-
-
|