Literature references that cite this PDB file's
key reference
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PubMed id
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Reference
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D.W.Wong
(2009).
Structure and action mechanism of ligninolytic enzymes.
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Appl Biochem Biotechnol, 157,
174-209.
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J.Yoon,
S.Fujii,
and
E.I.Solomon
(2009).
Geometric and electronic structure differences between the type 3 copper sites of the multicopper oxidases and hemocyanin/tyrosinase.
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| |
Proc Natl Acad Sci U S A, 106,
6585-6590.
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K.Hildén,
T.K.Hakala,
and
T.Lundell
(2009).
Thermotolerant and thermostable laccases.
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Biotechnol Lett, 31,
1117-1128.
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M.Andberg,
N.Hakulinen,
S.Auer,
M.Saloheimo,
A.Koivula,
J.Rouvinen,
and
K.Kruus
(2009).
Essential role of the C-terminus in Melanocarpus albomyces laccase for enzyme production, catalytic properties and structure.
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FEBS J, 276,
6285-6300.
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S.Ghosh,
X.Xie,
A.Dey,
Y.Sun,
C.P.Scholes,
and
E.I.Solomon
(2009).
Thermodynamic equilibrium between blue and green copper sites and the role of the protein in controlling function.
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Proc Natl Acad Sci U S A, 106,
4969-4974.
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T.J.Lawton,
L.A.Sayavedra-Soto,
D.J.Arp,
and
A.C.Rosenzweig
(2009).
Crystal structure of a two-domain multicopper oxidase: IMPLICATIONS FOR THE EVOLUTION OF MULTICOPPER BLUE PROTEINS.
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J Biol Chem, 284,
10174-10180.
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PDB code:
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Y.Shimazaki,
M.Takani,
and
O.Yamauchi
(2009).
Metal complexes of amino acids and amino acid side chain groups. Structures and properties.
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Dalton Trans, 0,
7854-7869.
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Z.Haibo,
Z.Yinglong,
H.Feng,
G.Peiji,
and
C.Jiachuan
(2009).
Purification and characterization of a thermostable laccase with unique oxidative characteristics from Trametes hirsuta.
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Biotechnol Lett, 31,
837-843.
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A.Kunamneni,
S.Camarero,
C.García-Burgos,
F.J.Plou,
A.Ballesteros,
and
M.Alcalde
(2008).
Engineering and Applications of fungal laccases for organic synthesis.
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Microb Cell Fact, 7,
32.
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G.Bleve,
C.Lezzi,
G.Mita,
P.Rampino,
C.Perrotta,
L.Villanova,
and
F.Grieco
(2008).
Molecular cloning and heterologous expression of a laccase gene from Pleurotus eryngii in free and immobilized Saccharomyces cerevisiae cells.
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Appl Microbiol Biotechnol, 79,
731-741.
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M.A.Tadesse,
A.D'Annibale,
C.Galli,
P.Gentili,
and
F.Sergi
(2008).
An assessment of the relative contributions of redox and steric issues to laccase specificity towards putative substrates.
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Org Biomol Chem, 6,
868-878.
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R.Wiener,
Y.Haitin,
L.Shamgar,
M.C.Fernández-Alonso,
A.Martos,
O.Chomsky-Hecht,
G.Rivas,
B.Attali,
and
J.A.Hirsch
(2008).
The KCNQ1 (Kv7.1) COOH terminus, a multitiered scaffold for subunit assembly and protein interaction.
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J Biol Chem, 283,
5815-5830.
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PDB code:
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M.Ferraroni,
N.M.Myasoedova,
V.Schmatchenko,
A.A.Leontievsky,
L.A.Golovleva,
A.Scozzafava,
and
F.Briganti
(2007).
Crystal structure of a blue laccase from Lentinus tigrinus: evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases.
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BMC Struct Biol, 7,
60.
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PDB code:
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O.V.Morozova,
G.P.Shumakovich,
M.A.Gorbacheva,
S.V.Shleev,
and
A.I.Yaropolov
(2007).
"Blue" laccases.
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Biochemistry (Mosc), 72,
1136-1150.
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S.R.Waterman,
M.Hacham,
J.Panepinto,
G.Hu,
S.Shin,
and
P.R.Williamson
(2007).
Cell wall targeting of laccase of Cryptococcus neoformans during infection of mice.
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Infect Immun, 75,
714-722.
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A.Beloqui,
M.Pita,
J.Polaina,
A.Martínez-Arias,
O.V.Golyshina,
M.Zumárraga,
M.M.Yakimov,
H.García-Arellano,
M.Alcalde,
V.M.Fernández,
K.Elborough,
J.M.Andreu,
A.Ballesteros,
F.J.Plou,
K.N.Timmis,
M.Ferrer,
and
P.N.Golyshin
(2006).
Novel polyphenol oxidase mined from a metagenome expression library of bovine rumen: biochemical properties, structural analysis, and phylogenetic relationships.
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J Biol Chem, 281,
22933-22942.
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A.Marjasvaara,
K.Kruus,
and
P.Vainiotalo
(2006).
A laccase study by electrospray ionization Fourier transform ion cyclotron resonance MS: copper depletion, glycoforms and stability.
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J Mass Spectrom, 41,
91-97.
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A.V.Lyashenko,
I.Bento,
V.N.Zaitsev,
N.E.Zhukhlistova,
Y.N.Zhukova,
A.G.Gabdoulkhakov,
E.Y.Morgunova,
W.Voelter,
G.S.Kachalova,
E.V.Stepanova,
O.V.Koroleva,
V.S.Lamzin,
V.I.Tishkov,
C.Betzel,
P.F.Lindley,
and
A.M.Mikhailov
(2006).
X-ray structural studies of the fungal laccase from Cerrena maxima.
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J Biol Inorg Chem, 11,
963-973.
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A.V.Lyashenko,
N.E.Zhukhlistova,
A.G.Gabdoulkhakov,
Y.N.Zhukova,
W.Voelter,
V.N.Zaitsev,
I.Bento,
E.V.Stepanova,
G.S.Kachalova,
O.V.Koroleva,
E.A.Cherkashyn,
V.I.Tishkov,
V.S.Lamzin,
K.Schirwitz,
E.Y.Morgunova,
C.Betzel,
P.F.Lindley,
and
A.M.Mikhailov
(2006).
Purification, crystallization and preliminary X-ray study of the fungal laccase from Cerrena maxima.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 62,
954-957.
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PDB code:
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P.Baldrian
(2006).
Fungal laccases - occurrence and properties.
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FEMS Microbiol Rev, 30,
215-242.
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P.J.Hoegger,
S.Kilaru,
T.Y.James,
J.R.Thacker,
and
U.Kües
(2006).
Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences.
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FEBS J, 273,
2308-2326.
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S.Kilaru,
P.J.Hoegger,
and
U.Kües
(2006).
The laccase multi-gene family in Coprinopsis cinerea has seventeen different members that divide into two distinct subfamilies.
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Curr Genet, 50,
45-60.
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S.Sakasegawa,
H.Ishikawa,
S.Imamura,
H.Sakuraba,
S.Goda,
and
T.Ohshima
(2006).
Bilirubin oxidase activity of Bacillus subtilis CotA.
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Appl Environ Microbiol, 72,
972-975.
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A.B.Taylor,
C.S.Stoj,
L.Ziegler,
D.J.Kosman,
and
P.J.Hart
(2005).
The copper-iron connection in biology: structure of the metallo-oxidase Fet3p.
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Proc Natl Acad Sci U S A, 102,
15459-15464.
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PDB code:
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G.Battistuzzi,
M.Bellei,
A.Leonardi,
R.Pierattelli,
A.De Candia,
A.J.Vila,
and
M.Sola
(2005).
Reduction thermodynamics of the T1 Cu site in plant and fungal laccases.
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J Biol Inorg Chem, 10,
867-873.
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I.Bento,
L.O.Martins,
G.Gato Lopes,
M.Arménia Carrondo,
and
P.F.Lindley
(2005).
Dioxygen reduction by multi-copper oxidases; a structural perspective.
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Dalton Trans, 0,
3507-3513.
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PDB codes:
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Y.Taprab,
T.Johjima,
Y.Maeda,
S.Moriya,
S.Trakulnaleamsai,
N.Noparatnaraporn,
M.Ohkuma,
and
T.Kudo
(2005).
Symbiotic fungi produce laccases potentially involved in phenol degradation in fungus combs of fungus-growing termites in Thailand.
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Appl Environ Microbiol, 71,
7696-7704.
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A.Marjasvaara,
M.Torvinen,
and
P.Vainiotalo
(2004).
Laccase-catalyzed mediated oxidation of benzyl alcohol: the role of TEMPO and formation of products including benzonitrile studied by nanoelectrospray ionization Fourier transform ion cyclotron resonance mass spectrometry.
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J Mass Spectrom, 39,
1139-1146.
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F.J.Enguita,
D.Marçal,
L.O.Martins,
R.Grenha,
A.O.Henriques,
P.F.Lindley,
and
M.A.Carrondo
(2004).
Substrate and dioxygen binding to the endospore coat laccase from Bacillus subtilis.
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J Biol Chem, 279,
23472-23476.
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PDB codes:
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F.J.Enguita,
L.O.Martins,
A.O.Henriques,
and
M.A.Carrondo
(2003).
Crystal structure of a bacterial endospore coat component. A laccase with enhanced thermostability properties.
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J Biol Chem, 278,
19416-19425.
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PDB code:
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L.F.Larrondo,
L.Salas,
F.Melo,
R.Vicuña,
and
D.Cullen
(2003).
A novel extracellular multicopper oxidase from Phanerochaete chrysosporium with ferroxidase activity.
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Appl Environ Microbiol, 69,
6257-6263.
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S.V.Kumar,
P.S.Phale,
S.Durani,
and
P.P.Wangikar
(2003).
Combined sequence and structure analysis of the fungal laccase family.
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Biotechnol Bioeng, 83,
386-394.
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A.E.Palmer,
L.Quintanar,
S.Severance,
T.P.Wang,
D.J.Kosman,
and
E.I.Solomon
(2002).
Spectroscopic characterization and O2 reactivity of the trinuclear Cu cluster of mutants of the multicopper oxidase Fet3p.
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Biochemistry, 41,
6438-6448.
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A.Klonowska,
C.Gaudin,
A.Fournel,
M.Asso,
J.Le Petit,
M.Giorgi,
and
T.Tron
(2002).
Characterization of a low redox potential laccase from the basidiomycete C30.
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Eur J Biochem, 269,
6119-6125.
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A.P.Litvintseva,
and
J.M.Henson
(2002).
Cloning, characterization, and transcription of three laccase genes from Gaeumannomyces graminis var. tritici, the take-all fungus.
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Appl Environ Microbiol, 68,
1305-1311.
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E.Record,
P.J.Punt,
M.Chamkha,
M.Labat,
C.A.van Den Hondel,
and
M.Asther
(2002).
Expression of the Pycnoporus cinnabarinus laccase gene in Aspergillus niger and characterization of the recombinant enzyme.
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Eur J Biochem, 269,
602-609.
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F.Hong,
N.Q.Meinander,
and
L.J.Jönsson
(2002).
Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris.
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Biotechnol Bioeng, 79,
438-449.
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K.Piontek,
M.Antorini,
and
T.Choinowski
(2002).
Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers.
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J Biol Chem, 277,
37663-37669.
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PDB code:
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L.O.Martins,
C.M.Soares,
M.M.Pereira,
M.Teixeira,
T.Costa,
G.H.Jones,
and
A.O.Henriques
(2002).
Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat.
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J Biol Chem, 277,
18849-18859.
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N.Hakulinen,
L.L.Kiiskinen,
K.Kruus,
M.Saloheimo,
A.Paananen,
A.Koivula,
and
J.Rouvinen
(2002).
Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site.
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Nat Struct Biol, 9,
601-605.
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PDB code:
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P.Vachette,
E.Dainese,
V.B.Vasyliev,
P.Di Muro,
M.Beltramini,
D.I.Svergun,
V.De Filippis,
and
B.Salvato
(2002).
A key structural role for active site type 3 copper ions in human ceruloplasmin.
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J Biol Chem, 277,
40823-40831.
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S.A.Roberts,
A.Weichsel,
G.Grass,
K.Thakali,
J.T.Hazzard,
G.Tollin,
C.Rensing,
and
W.R.Montfort
(2002).
Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli.
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Proc Natl Acad Sci U S A, 99,
2766-2771.
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PDB code:
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T.Bertrand,
C.Jolivalt,
P.Briozzo,
E.Caminade,
N.Joly,
C.Madzak,
and
C.Mougin
(2002).
Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics.
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Biochemistry, 41,
7325-7333.
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PDB code:
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A.Donaire,
B.Jiménez,
J.Moratal,
J.F.Hall,
and
S.S.Hasnain
(2001).
Electronic characterization of the oxidized state of the blue copper protein rusticyanin by 1H NMR: is the axial methionine the dominant influence for the high redox potential?
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Biochemistry, 40,
837-846.
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C.Kim,
W.W.Lorenz,
J.T.Hoopes,
and
J.F.Dean
(2001).
Oxidation of phenolate siderophores by the multicopper oxidase encoded by the Escherichia coli yacK gene.
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J Bacteriol, 183,
4866-4875.
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E.I.Solomon,
P.Chen,
M.Metz,
S.K.Lee,
and
A.E.Palmer
(2001).
Oxygen Binding, Activation, and Reduction to Water by Copper Proteins.
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| |
Angew Chem Int Ed Engl, 40,
4570-4590.
|
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H.Hoshida,
M.Nakao,
H.Kanazawa,
K.Kubo,
T.Hakukawa,
K.Morimasa,
R.Akada,
and
Y.Nishizawa
(2001).
Isolation of five laccase gene sequences from the white-rot fungus Trametes sanguinea by PCR, and cloning, characterization and expression of the laccase cDNA in yeasts.
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| |
J Biosci Bioeng, 92,
372-380.
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L.Otterbein,
E.Record,
S.Longhi,
M.Asther,
and
S.Moukha
(2000).
Molecular cloning of the cDNA encoding laccase from Pycnoporus cinnabarinus I-937 and expression in Pichia pastoris.
|
| |
Eur J Biochem, 267,
1619-1625.
|
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M.J.Colaneri,
J.Vitali,
and
J.Peisach
(2000).
Electron spin-echo envelope modulation study of multicrystalline Cu(2+)-insulin: effects of Cd(2+) on the nuclear quadrupole interaction of the Cu(2+)-coordinated imidazole remote nitrogen.
|
| |
Biochemistry, 39,
584-591.
|
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N.J.Blackburn,
M.Ralle,
R.Hassett,
and
D.J.Kosman
(2000).
Spectroscopic analysis of the trinuclear cluster in the Fet3 protein from yeast, a multinuclear copper oxidase.
|
| |
Biochemistry, 39,
2316-2324.
|
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U.Kües
(2000).
Life history and developmental processes in the basidiomycete Coprinus cinereus.
|
| |
Microbiol Mol Biol Rev, 64,
316-353.
|
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A.Shimizu,
J.H.Kwon,
T.Sasaki,
T.Satoh,
N.Sakurai,
T.Sakurai,
S.Yamaguchi,
and
T.Samejima
(1999).
Myrothecium verrucaria bilirubin oxidase and its mutants for potential copper ligands.
|
| |
Biochemistry, 38,
3034-3042.
|
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D.S.Yaver,
M.D.Overjero,
F.Xu,
B.A.Nelson,
K.M.Brown,
T.Halkier,
S.Bernauer,
S.H.Brown,
and
S.Kauppinen
(1999).
Molecular characterization of laccase genes from the basidiomycete Coprinus cinereus and heterologous expression of the laccase lcc1.
|
| |
Appl Environ Microbiol, 65,
4943-4948.
|
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F.Xu,
A.E.Palmer,
D.S.Yaver,
R.M.Berka,
G.A.Gambetta,
S.H.Brown,
and
E.I.Solomon
(1999).
Targeted mutations in a Trametes villosa laccase. Axial perturbations of the T1 copper.
|
| |
J Biol Chem, 274,
12372-12375.
|
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G.Alexandre,
R.Bally,
B.L.Taylor,
and
I.B.Zhulin
(1999).
Loss of cytochrome c oxidase activity and acquisition of resistance to quinone analogs in a laccase-positive variant of Azospirillum lipoferum.
|
| |
J Bacteriol, 181,
6730-6738.
|
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H.Huang,
G.Zoppellaro,
and
T.Sakurai
(1999).
Spectroscopic and kinetic studies on the oxygen-centered radical formed during the four-electron reduction process of dioxygen by Rhus vernicifera laccase.
|
| |
J Biol Chem, 274,
32718-32724.
|
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I.Gromov,
A.Marchesini,
O.Farver,
I.Pecht,
and
D.Goldfarb
(1999).
Azide binding to the trinuclear copper center in laccase and ascorbate oxidase.
|
| |
Eur J Biochem, 266,
820-830.
|
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I.Masuda-Nishimura,
K.Ichikawa,
O.Hatamoto,
K.Abe,
and
Y.Koyama
(1999).
cDNA cloning of bilirubin oxidase from Pleurotus ostreatus strain Shinshu and its expression in Aspergillus sojae: an efficient screening of transformants, using the laccase activity of bilirubin oxidase.
|
| |
J Gen Appl Microbiol, 45,
93-97.
|
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J.Zhao,
and
H.S.Kwan
(1999).
Characterization, molecular cloning, and differential expression analysis of laccase genes from the edible mushroom Lentinula edodes.
|
| |
Appl Environ Microbiol, 65,
4908-4913.
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M.Gelo-Pujic,
H.H.Kim,
N.G.Butlin,
and
G.T.Palmore
(1999).
Electrochemical studies of a truncated laccase produced in Pichia pastoris.
|
| |
Appl Environ Microbiol, 65,
5515-5521.
|
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O.Farver,
L.Bendahl,
L.K.Skov,
and
I.Pecht
(1999).
Human ceruloplasmin. Intramolecular electron transfer kinetics and equilibration.
|
| |
J Biol Chem, 274,
26135-26140.
|
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|
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T.E.Machonkin,
H.H.Zhang,
B.Hedman,
K.O.Hodgson,
and
E.I.Solomon
(1998).
Spectroscopic and magnetic studies of human ceruloplasmin: identification of a redox-inactive reduced Type 1 copper site.
|
| |
Biochemistry, 37,
9570-9578.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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