Indexed keywords
METHYLOCOCCUS CAPSULATUS;
IRON;
LIGAND;
METHANE MONOOXYGENASE;
OXYGENASE;
BINDING SITE;
CATALYSIS;
CHEMISTRY;
ERRATUM;
HYDROXYLATION;
OXIDATION REDUCTION REACTION;
ULTRASTRUCTURE;
X RAY CRYSTALLOGRAPHY;
ARTICLE;
BINDING SITES;
CATALYSIS;
CRYSTALLOGRAPHY, X-RAY;
HYDROXYLATION;
IRON;
LIGANDS;
OXIDATION-REDUCTION;
OXYGENASES;
SUPPORT, NON-U.S. GOV'T;
SUPPORT, U.S. GOV'T, P.H.S.;
2
0000950578
Determining the structure of a hydroxylase enzyme that catalyzes the conversion of methane to methanol in methanotrophic bacteria
(1994)
Accounts Chem. Res.
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, pp. 229-236
Rosenzweig1
Lippard2
3
0001618049
Studies of the soluble methane monooxygenase protein system: structure, component interactions, and hydroxylation mechanism
in press
(1995)
Adv. Inorg. Chem.
Liu1
Lippard2
7
0029167778
Characterizaton of a diiron(III) peroxo intermediate in the reaction cycle of methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)
(1995)
J. Am. Chem. Soc.
, vol.117
, pp. 4987-4990
Liu1
Lippard2
8
0009411657
Reactions of non-heme iron(II) complexes with dioxygen in chemistry and biology
(1994)
Chem. Rev.
, vol.94
, pp. 759-805
Feig1
Lippard2
10
0000200442
Proton ENDOR identification of bridging hydroxide ligands in mixed-valent diiron centers of proteins: methane monooxygenase and semimet aziclohemerythrin
(1993)
J. Am. Chem. Soc.
, vol.115
, pp. 6440-6441
DeRose1
Liu2
Lippard3
Hoffman4
11
0000139525
X-ray absorption, Mössbauer, and EPR studies of the dinuclear iron center in the hydroxylase component of methane monooxygenase
(1991)
J. Am. Chem. Soc.
, vol.113
, pp. 9219-9235
DeWitt1
Lippard2
13
0027849663
Spectroscopic studies of the coupled binuclear non-heme iron active site in the fully reduced hydroxylase component of methane monooxygenase: comparison to deoxy and cleoxy-azide hemerythrin
(1993)
J. Am. Chem. Soc.
, vol.115
, pp. 12409-12422
Pulver1
Froland2
Fox3
Lipscomb4
Solomon5
15
0001503269
Monodentate carboxylate complexes and the carboxylate shift: implications for polymetalloprotein structure and function
(1991)
New. J. Chem.
, vol.15
, pp. 417-430
Rardin1
Tolman2
Lippard3
16
0026062115
Models of the reduced forms of polyiron-oxo proteins: an asymmetric, triply carboxylate bridged diiron(II) complex and its reaction with dioxygen
(1991)
J. Am. Chem. Soc.
, vol.113
, pp. 152-164
Tolman1
Liu2
Bentsen3
Lippard4
19
0025214461
Ribonucleotide reductases: amazing and confusing
(1990)
J. Biol. Chem.
, vol.265
, pp. 5329-5332
Stubbe1
20
0025293287
Three dimensional structure of the free radical protein of ribonucleotide reductase
(1990)
Nature
, vol.345
, pp. 593-598
Nordlund1
Sjöberg2
Eklund3
21
8944251805
Ribonucleotide reductase from Escherichia coli: structural aspects of protein function
Stockholm University
(1993)
Ph.D. thesis
Åberg1
22
0027283896
Structure and function of the Escherichia coli ribonucleotide reductase protein R2
(1993)
J. Mol. Biol.
, vol.232
, pp. 123-164
Nordlund1
Eklund2
23
0025766709
Redox properties of the hydroxylase component of methane monooxygenase from Methylococcus capsulatus (Bath)
(1991)
J. Biol. Chem.
, vol.266
, pp. 12836-12839
Liu1
Lippard2
24
0026321616
Redox properties of the hydroxylase component of methane monooxygenase from Methylococcus capsulatus (Bath)
(1991)
J. Biol. Chem.
, vol.266
, pp. 24859
Liu1
Lippard2
27
0026088028
Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b
(1991)
J. Biol. Chem.
, vol.266
, pp. 540-550
Fox1
Liu2
Dege3
Lipscomb4
35
0026671893
Crystallization and preliminary X-ray analysis of the methane monooxygenase hydroxylase protein from Methylococcus capsulatus (Bath)
(1992)
J. Mol. Biol.
, vol.227
, pp. 283-285
Rosenzweig1
Frederick2
Lippard3
39
0001099937
Traitement statistique des erreurs clans la determination des structures cristallines
(1952)
Acta Crystallographica
, vol.5
, pp. 802-810
Luzatti1