DB code: S00925

CATH domain 1.10.1280.10 : di-copper center containing domain from catechol oxidase Catalytic domain
E.C. 1.14.18.1
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
B2ZB02
Tyrosinase
PF00264 (Tyrosinase)
[Graphical View]
Q83WS2
Tyrosinase
PF00264 (Tyrosinase)
[Graphical View]

KEGG enzyme name
Tyrosinase
Monophenol monooxygenase
Phenolase
Monophenol oxidase
Cresolase
Monophenolase
Tyrosine-dopa oxidase
Monophenol monooxidase
Monophenol dihydroxyphenylalanine:oxygen oxidoreductase
N-acetyl-6-hydroxytryptophan oxidase
Monophenol, dihydroxy-L-phenylalanine oxygen oxidoreductase
O-diphenol:O2 oxidoreductase
Phenol oxidase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
B2ZB02 B2ZB02_BACME
Q83WS2 Q83WS2_9ACTO

KEGG Pathways
Map code Pathways E.C.
MAP00350 Tyrosine metabolism
MAP00740 Riboflavin metabolism
MAP00950 Isoquinoline alkaloid biosynthesis
MAP00965 Betalain biosynthesis
MAP01110 Biosynthesis of secondary metabolites

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00070 C00082 C00007 C00355 C00355 C00822 C00001
E.C.
Compound Copper L-tyrosine O2 L-dopa L-dopa dopaquinone H2O
Type heavy metal amino acids,aromatic ring (only carbon atom) others amino acids,aromatic ring (only carbon atom) amino acids,aromatic ring (only carbon atom) amino acids,aromatic ring (only carbon atom) H2O
ChEBI 28694
 30052
 28694
 30052
 		17895
 58315
 17895
 58315
 		15379
 26689
 27140
 15379
 26689
 27140
 		15765
 57504
 15765
 57504
 		15765
 57504
 15765
 57504
 		16852
 57924
 16852
 57924
 		15377
 15377
PubChem 23978
 23978
 		6057
 6942100
 6057
 6942100
 		977
 977
 		6047
 6971033
 6047
 6971033
 		6047
 6971033
 6047
 6971033
 		439316
 44229226
 439316
 44229226
 		22247451
 962
 22247451
 962
3nm8A Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
3nm8B Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
3npyA Bound:4x_CU Unbound Unbound Unbound Unbound Unbound
3npyB Bound:4x_CU Unbound Unbound Unbound Unbound Unbound
3nq0A Bound:_CU Unbound Unbound Unbound Unbound Unbound
3nq0B Bound:_CU Unbound Unbound Unbound Unbound Unbound
3nq1A Bound:2x_CU Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:KOJ
3nq1B Bound:2x_CU Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:KOJ
3nq5A Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
3nq5B Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
3ntmA Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
3ntmB Bound:_CU Unbound Unbound Unbound Unbound Unbound
4d87A Bound:_CU Unbound Unbound Unbound Unbound Unbound
4d87B Bound:_CU Unbound Unbound Unbound Unbound Unbound
4hd4A Bound:_CU Unbound Unbound Unbound Unbound Unbound
4hd4B Bound:_CU Unbound Unbound Unbound Unbound Unbound
4hd6A Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
4hd6B Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
4hd7A Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
4hd7B Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
1wx2A Bound:2x_CU Unbound Analogue:PER Unbound Unbound Unbound
1wx4A Bound:2x_CU Unbound Analogue:PER Unbound Unbound Unbound
1wx5A Unbound Unbound Unbound Unbound Unbound Unbound
1wx5C Unbound Unbound Unbound Unbound Unbound Unbound
1wxcA Unbound Unbound Unbound Unbound Unbound Unbound
2ahkA Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
2ahlA Bound:2xCU1 Unbound Unbound Unbound Unbound Unbound
2zmxA Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
2zmyA Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
2zmzA Bound:2xCU1 Unbound Unbound Unbound Unbound Unbound
2zwdA Bound:3xCU1 Unbound Unbound Unbound Unbound Unbound
2zweA Bound:3x_CU Unbound Unbound Unbound Analogue:DAH(chain B) Unbound
2zwfA Bound:3x_CU Unbound Unbound Unbound Analogue:DAH(chain B) Unbound
2zwgA Bound:3x_CU Unbound Unbound Unbound Analogue:DAH(chain B) Unbound
3awsA Bound:_CU Unbound Unbound Unbound Unbound Unbound
3awtA Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
3awuA Bound:3x_CU Unbound Unbound Unbound Unbound Unbound
3awvA Bound:2x_CU Unbound Unbound Unbound Unbound Unbound
3awwA Bound:3x_CU Unbound Unbound Unbound Unbound Unbound
3awxA Bound:3x_CU Unbound Unbound Unbound Unbound Unbound
3awyA Bound:3x_CU Unbound Unbound Unbound Unbound Unbound
3awzA Bound:_CU Unbound Unbound Unbound Unbound Unbound
3ax0A Bound:2x_CU Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [14], [22], [25]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
3nm8A HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) Met I form?
3nm8B HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) Met I form?
3npyA HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) Met I form
3npyB HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) Met I form
3nq0A HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
3nq0B HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
3nq1A HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) Met I form
3nq1B HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) Met I form
3nq5A HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) mutant R209H, Deoxy reduced form
3nq5B HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) mutant R209H, Deoxy reduced form
3ntmA HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) Met I form
3ntmB HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
4d87A HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
4d87B HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding)
4hd4A HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) mutant V218F
4hd4B HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) mutant V218F
4hd6A HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) mutant V218F, Met I form?
4hd6B HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) mutant V218F, Met I form
4hd7A HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) mutant V218G, Met I form
4hd7B HIS 42;HIS 60;HIS 69(Copper-1 binding);HIS 204;HIS 208;HIS 231(Copper-2 binding) mutant V218G, Met I form?
1wx2A HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Oxy oxidized form
1wx4A HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Oxy oxidized form
1wx5A HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
1wx5C HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
1wxcA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
2ahkA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Met II form
2ahlA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Deoxy reduced form
2zmxA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Met I form
2zmyA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Met II form
2zmzA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Deoxy reduced form
2zwdA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Deoxy reduced form?
2zweA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Met I form
2zwfA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Met I form
2zwgA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Met II form
3awsA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
3awtA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Met I form
3awuA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Met I form
3awvA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Met II form
3awwA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Met II form?
3awxA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Met II form?
3awyA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Met II form?
3awzA HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding)
3ax0A HIS 38;HIS 54;HIS 63(Copper-1 binding);HIS 190;HIS 194;HIS 216(Copper-2 binding) Met I form

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[14]
Fig. 9, p.8989
[15]
Scheme 2, p.4550
[20]
Fig. 2, p.754-756
[22]
Fig. 17, p.124-127
[23]
Scheme 2, p.73-74
[25]
p.232-234

References
[1]
Resource
Comments
Medline ID
PubMed ID 2846043
Journal Biochemistry
Year 1988
Volume 27
Pages 5610-5
Authors Huber M, Lerch K
Title Identification of two histidines as copper ligands in Streptomyces glaucescens tyrosinase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 3130643
Journal Prog Clin Biol Res
Year 1988
Volume 256
Pages 85-98
Authors Lerch K
Title Protein and active-site structure of tyrosinase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 1348173
Journal Biochem J
Year 1992
Volume 282
Pages 915-8
Authors Jackman MP, Huber M, Hajnal A, Lerch K
Title Stabilization of the oxy form of tyrosinase by a single conservative amino acid substitution.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 7873577
Journal Biochim Biophys Acta
Year 1995
Volume 1247
Pages 1-11
Authors Sanchez-Ferrer A, Rodriguez-Lopez JN, Garcia-Canovas F, Garcia-Carmona F
Title Tyrosinase: a comprehensive review of its mechanism.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 9668113
Journal J Biol Chem
Year 1998
Volume 273
Pages 19243-50
Authors Tsai TY, Lee YH
Title Roles of copper ligands in the activation and secretion of Streptomyces tyrosinase.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 9929004
Journal FEBS Lett
Year 1999
Volume 442
Pages 215-20
Authors Bubacco L, Salgado J, Tepper AW, Vijgenboom E, Canters GW
Title 1H NMR spectroscopy of the binuclear Cu(II) active site of Streptomyces antibioticus tyrosinase.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10838090
Journal FEBS Lett
Year 2000
Volume 474
Pages 228-32
Authors van Gastel M, Bubacco L, Groenen EJ, Vijgenboom E, Canters GW
Title EPR study of the dinuclear active copper site of tyrosinase from Streptomyces antibioticus.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 12235154
Journal J Biol Chem
Year 2002
Volume 277
Pages 44606-12
Authors Battaini G, Monzani E, Casella L, Lonardi E, Tepper AW, Canters GW, Bubacco L
Title Tyrosinase-catalyzed oxidation of fluorophenols.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 12048185
Journal J Biol Chem
Year 2002
Volume 277
Pages 30436-44
Authors Tepper AW, Bubacco L, Canters GW
Title Structural basis and mechanism of the inhibition of the type-3 copper protein tyrosinase from Streptomyces antibioticus by halide ions.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 12028580
Journal Pigment Cell Res
Year 2002
Volume 15
Pages 162-73
Authors Garcia-Borron JC, Solano F
Title Molecular anatomy of tyrosinase and its related proteins: beyond the histidine-bound metal catalytic center.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 12473668
Journal J Biol Chem
Year 2003
Volume 278
Pages 7381-9
Authors Bubacco L, Van Gastel M, Groenen EJ, Vijgenboom E, Canters GW
Title Spectroscopic characterization of the electronic changes in the active site of Streptomyces antibioticus tyrosinase upon binding of transition state analogue inhibitors.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 15643881
Journal J Am Chem Soc
Year 2005
Volume 127
Pages 567-75
Authors Tepper AW, Bubacco L, Canters GW
Title Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 16927257
Journal Chemistry
Year 2006
Volume 12
Pages 7668-75
Authors Tepper AW, Bubacco L, Canters GW
Title Paramagnetic properties of the halide-bound derivatives of oxidised tyrosinase investigated by 1H NMR spectroscopy.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH COPPER.
Medline ID
PubMed ID 16436386
Journal J Biol Chem
Year 2006
Volume 281
Pages 8981-90
Authors Matoba Y, Kumagai T, Yamamoto A, Yoshitsu H, Sugiyama M
Title Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis.
Related PDB 1wx2 1wx4 1wx5 1wxc 2ahk 2ahl 2zmx
Related UniProtKB Q83WS2
[15]
Resource
Comments
Medline ID
PubMed ID 16795103
Journal Angew Chem Int Ed Engl
Year 2006
Volume 45
Pages 4546-50
Authors Decker H, Schweikardt T, Tuczek F
Title The first crystal structure of tyrosinase: all questions answered?
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 16403014
Journal FEBS J
Year 2006
Volume 273
Pages 257-70
Authors Hernandez-Romero D, Sanchez-Amat A, Solano F
Title A tyrosinase with an abnormally high tyrosine hydroxylase/dopa oxidase ratio.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 17698026
Journal Arch Biochem Biophys
Year 2007
Volume 465
Pages 320-7
Authors Bubacco L, Spinazze R, della Longa S, Benfatto M
Title X-ray absorption analysis of the active site of Streptomyces antibioticus Tyrosinase upon binding of transition state analogue inhibitors.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 18336914
Journal J Inorg Biochem
Year 2008
Volume 102
Pages 1170-89
Authors De A, Mandal S, Mukherjee R
Title Modeling tyrosinase activity. Effect of ligand topology on aromatic ring hydroxylation: an overview.
Related PDB
Related UniProtKB
[19]
Resource
Comments NUCLEOTIDE SEQUENCE.
Medline ID
PubMed ID 19672047
Journal J Mol Microbiol Biotechnol
Year 2009
Volume 17
Pages 188-200
Authors Shuster V, Fishman A
Title Isolation, cloning and characterization of a tyrosinase with improved activity in organic solvents from Bacillus megaterium.
Related PDB
Related UniProtKB B2ZB02
[20]
Resource
Comments
Medline ID
PubMed ID 19735457
Journal Pigment Cell Melanoma Res
Year 2009
Volume 22
Pages 750-60
Authors Olivares C, Solano F
Title New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 20823537
Journal Acta Crystallogr Sect F Struct Biol Cryst Commun
Year 2010
Volume 66
Pages 1101-3
Authors Sendovski M, Kanteev M, Shuster Ben-Yosef V, Adir N, Fishman A
Title Crystallization and preliminary X-ray crystallographic analysis of a bacterial tyrosinase from Bacillus megaterium.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 19690900
Journal J Biol Inorg Chem
Year 2010
Volume 15
Pages 117-29
Authors Deeth RJ, Diedrich C
Title Structural and mechanistic insights into the oxy form of tyrosinase from molecular dynamics simulations.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 20875779
Journal Arch Biochem Biophys
Year 2011
Volume 505
Pages 67-74
Authors Marino SM, Fogal S, Bisaglia M, Moro S, Scartabelli G, De Gioia L, Spada A, Monzani E, Casella L, Mammi S, Bubacco L
Title Investigation of Streptomyces antibioticus tyrosinase reactivity toward chlorophenols.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 21730070
Journal J Biol Chem
Year 2011
Volume 286
Pages 30219-31
Authors Matoba Y, Bando N, Oda K, Noda M, Higashikawa F, Kumagai T, Sugiyama M
Title A molecular mechanism for copper transportation to tyrosinase that is assisted by a metallochaperone, caddie protein.
Related PDB 3aws 3awt 3awu 3awv 3aww 3awx 3awy 3awz 3ax0
Related UniProtKB
[25]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC.
Medline ID
PubMed ID 21040728
Journal J Mol Biol
Year 2011
Volume 405
Pages 227-37
Authors Sendovski M, Kanteev M, Ben-Yosef VS, Adir N, Fishman A
Title First structures of an active bacterial tyrosinase reveal copper plasticity.
Related PDB 3nm8 3npy 3nq0 3nq1 3nq5 3ntm
Related UniProtKB B2ZB02
[26]
Resource
Comments
Medline ID
PubMed ID 22539021
Journal Appl Microbiol Biotechnol
Year 2013
Volume 97
Pages 1953-61
Authors Goldfeder M, Egozy M, Shuster Ben-Yosef V, Adir N, Fishman A
Title Changes in tyrosinase specificity by ionic liquids and sodium dodecyl sulfate.
Related PDB 4d87
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 23305929
Journal Biochim Biophys Acta
Year 2013
Volume 1834
Pages 629-33
Authors Goldfeder M, Kanteev M, Adir N, Fishman A
Title Influencing the monophenolase/diphenolase activity ratio in tyrosinase.
Related PDB 4hd4 4hd6 4hd7
Related UniProtKB

Comments
This enzyme catalyzes the two distinct reactions as follows:
(1) L-tyrosine + 1/2 O2 = L-dopa (ortho hydroxylation of monophenol; monophenolase activity)
(2) L-dopa + 1/2 O2 = dopaquinone + H2O (two-electron oxidation of ortho-diphenol; diphenolase activity)
This enzyme belongs to the type-3 copper protein family, which includes hemocyanin and catechol oxidase (EC 1.10.3.1). The type-3 copper proteins contain a binuclear copper active site, which consists of two closely spaced copper atoms each coordinated by three histidine residues (see [10], [12], [14]). Catechol oxidase can catalyze only oxydation of ortho-diphenol, but lacks hydroxylation activity for monophenol.
According to the literature, the dinuclear copper active site exists in three redox forms:
(a) The deoxy (reduced) form [Cu(I)-Cu(I)];
(b) The oxy (oxidized) form [Cu(II)-O2(2-)-Cu(II)]; Molecular oxygen is bound as peroxide in a side-on bridging mode.
(c) The met (resting) form [Cu(II)-OH(-)-Cu(II)]; Cu(II) ions are bridged to either a water molecule or hydroxide ion.
The deoxy form can bind a molecular oxygen to give the oxy form.
Moreover, there is another redox form, half-met form [Cu(I)-OH(-)-Cu(II)], which is EPR active (see [12]). In this form, one of the two coppers is in the oxidized form.
According to the literature [15] and [22], the met form can be categorized into two types: met I with a single bridging ligand, and met II with two bridging ones.
Here, CuA is coordinated by His42, His60 and His69 (of 3nm8 in PDB), whereas CuB is coordinated by His His204, His208 and His231. There has been long-standing debate on whether substrate hydroxyl groups bind to CuA or CuB, particluarly for monophenolase reaction. The literature ([15], [20], [22] and [25]) supports the mechanism in which monophenol hydroxyl group is bound to CuA, whereas other reports ([12], [14] and [23]) suggest that monophenol docks to CuB.

Created Updated
2013-07-09 2013-07-24