DB code: T00024

RLCP classification 10.21001.100.10900 : Electron transfer
10.21021.100.10205 : Electron transfer
CATH domain 3.90.380.10 : Naphthalene 1,2-dioxygenase Alpha Subunit; Chain A, domain 1 Catalytic domain
2.102.10.10 : Rieske Iron-sulfur Protein Catalytic domain
3.10.450.50 : Nuclear Transport Factor 2; Chain
E.C. 1.14.12.12
CSA 1ndo
M-CSA 1ndo
MACiE M0130

CATH domain Related DB codes (homologues)
2.102.10.10 : Rieske Iron-sulfur Protein M00222
3.10.450.50 : Nuclear Transport Factor 2; Chain S00176 S00545 S00177

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0A110 Naphthalene 1,2-dioxygenase subunit alpha
EC 1.14.12.12
Naphthalene 1,2-dioxygenase ISP alpha
NP_863072.1 (Protein)
NC_004999.1 (DNA/RNA sequence)
YP_534822.1 (Protein)
NC_007926.1 (DNA/RNA sequence)
PF00355 (Rieske)
PF00848 (Ring_hydroxyl_A)
[Graphical View]
P0A111 Naphthalene 1,2-dioxygenase subunit alpha
EC 1.14.12.12
Naphthalene 1,2-dioxygenase ISP alpha
PF00355 (Rieske)
PF00848 (Ring_hydroxyl_A)
[Graphical View]
P0A112 Naphthalene 1,2-dioxygenase subunit beta
EC 1.14.12.12
Naphthalene 1,2-dioxygenase ISP beta
NP_863073.1 (Protein)
NC_004999.1 (DNA/RNA sequence)
YP_534823.1 (Protein)
NC_007926.1 (DNA/RNA sequence)
PF00866 (Ring_hydroxyl_B)
[Graphical View]
P0A113 Naphthalene 1,2-dioxygenase subunit beta
EC 1.14.12.12
Naphthalene 1,2-dioxygenase ISP beta
PF00866 (Ring_hydroxyl_B)
[Graphical View]

KEGG enzyme name
naphthalene 1,2-dioxygenase
naphthalene dioxygenase
naphthalene oxygenase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0A110 NDOB_PSEPU Naphthalene + NADH + O(2) = (1R,2S)-1,2- dihydronaphthalene-1,2-diol + NAD(+). Naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and an iron sulfur protein (ISP). The electron transfer component is composed of ferredoxin reductase (ndoR) and ferredoxin (ndoA), and ISP is composed of a large alpha subunit (ndoB) and a small beta subunit (ndoC). Binds 1 2Fe-2S cluster (Probable). Binds 1 iron ion (Probable).
P0A111 NDOB_PSEU8 Naphthalene + NADH + O(2) = (1R,2S)-1,2- dihydronaphthalene-1,2-diol + NAD(+). Naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and an iron sulfur protein (ISP). The electron transfer component is composed of ferredoxin reductase and ferredoxin (doxA), and ISP is composed of a large alpha subunit (doxB) and a small beta subunit (doxD) (Probable). Binds 1 2Fe-2S cluster (By similarity). Binds 1 iron ion (By similarity).
P0A112 NDOC_PSEPU Naphthalene + NADH + O(2) = (1R,2S)-1,2- dihydronaphthalene-1,2-diol + NAD(+). The naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and an iron sulfur protein (ISP). The electron transfer component is composed of ferredoxin reductase (ndoR) and ferredoxin (ndoA), and ISP is composed of a hexamer of three large alpha subunits (ndoB) and three small beta subunits (ndoC). Binds 1 2Fe-2S cluster (Probable). Binds 1 iron ion (Probable).
P0A113 NDOC_PSEU8 Naphthalene + NADH + O(2) = (1R,2S)-1,2- dihydronaphthalene-1,2-diol + NAD(+). Naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and an iron sulfur protein (ISP). The electron transfer component is composed of ferredoxin reductase and ferredoxin (doxA), and ISP is composed of a large alpha subunit (doxB) and a small beta subunit (doxD) (Probable). Binds 1 2Fe-2S cluster (By similarity). Binds 1 iron ion (By similarity).

KEGG Pathways
Map code Pathways E.C.
MAP00624 1- and 2-Methylnaphthalene degradation
MAP00626 Naphthalene and anthracene degradation
MAP00628 Fluorene degradation
MAP00642 Ethylbenzene degradation

Compound table
Cofactors Substrates Products Intermediates
KEGG-id L00023 C00023 C00829 C00004 C00007 C00080 C04314 C00003
E.C.
Compound [2Fe-2S] Iron Naphthalene NADH O2 H+ (1R,2S)-1,2-dihydronaphthalene-1,2-diol NAD+
Type heavy metal,sulfide group heavy metal aromatic ring (only carbon atom) amide group,amine group,nucleotide others others aromatic ring (only carbon atom),carbohydrate amide group,amine group,nucleotide
ChEBI 33739
18248
82664
16482
16908
15379
26689
27140
15378
44343
15846
PubChem 23925
931
439153
977
1038
440294
5893
1eg9A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:_FE Analogue:IND Unbound Unbound Unbound Unbound
1ndoA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:_FE Unbound Unbound Unbound Unbound Unbound
1ndoC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:_FE Unbound Unbound Unbound Unbound Unbound
1ndoE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:_FE Unbound Unbound Unbound Unbound Unbound
1o7gA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:_FE Bound:NPY Unbound Unbound Unbound Unbound
1o7hA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:_FE Unbound Unbound Unbound Unbound Unbound
1o7mA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:_FE Unbound Unbound Bound:OXY Unbound Unbound
1o7nA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:_FE Analogue:IND Unbound Bound:OXY Unbound Unbound
1o7pA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:_FE Unbound Unbound Unbound Bound:NDH Unbound
1o7wA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:_FE Unbound Unbound Unbound Unbound Unbound
1uuvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:_FE Analogue:IND Unbound Analogue:_NO Unbound Unbound
1uuwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:_FE Unbound Unbound Analogue:_NO Unbound Unbound
1eg9A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FES Unbound Unbound Unbound Unbound Unbound Unbound
1ndoA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FES Unbound Unbound Unbound Unbound Unbound Unbound
1ndoC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FES Unbound Unbound Unbound Unbound Unbound Unbound
1ndoE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FES Unbound Unbound Unbound Unbound Unbound Unbound
1o7gA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FES Unbound Unbound Unbound Unbound Unbound Unbound
1o7hA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FES Unbound Unbound Unbound Unbound Unbound Unbound
1o7mA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FES Unbound Unbound Unbound Unbound Unbound Unbound
1o7nA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FES Unbound Unbound Unbound Unbound Unbound Unbound
1o7pA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FES Unbound Unbound Unbound Unbound Unbound Unbound
1o7wA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FES Unbound Unbound Unbound Unbound Unbound Unbound
1uuvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FES Unbound Unbound Unbound Unbound Unbound Unbound
1uuwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FES Unbound Unbound Unbound Unbound Unbound Unbound
1eg9B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ndoB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ndoD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ndoF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o7gB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o7hB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o7mB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o7nB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o7pB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o7wB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1uuvB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1uuwB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P0A110, P0A111 & literature [4], [7], [9], [11], [17], [18]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1eg9A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 205;HIS 208 HIS 208;HIS 213;ASP 362(Iron binding)
1ndoA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 205;HIS 208 HIS 208;HIS 213;ASP 362(Iron binding)
1ndoC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 205;HIS 208 HIS 208;HIS 213;ASP 362(Iron binding)
1ndoE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 205;HIS 208 HIS 208;HIS 213;ASP 362(Iron binding)
1o7gA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 205;HIS 208 HIS 208;HIS 213;ASP 362(Iron binding)
1o7hA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 205;HIS 208 HIS 208;HIS 213;ASP 362(Iron binding)
1o7mA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 205;HIS 208 HIS 208;HIS 213;ASP 362(Iron binding)
1o7nA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 205;HIS 208 HIS 208;HIS 213;ASP 362(Iron binding)
1o7pA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 205;HIS 208 HIS 208;HIS 213;ASP 362(Iron binding)
1o7wA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 205;HIS 208 HIS 208;HIS 213;ASP 362(Iron binding)
1uuvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 205;HIS 208 HIS 208;HIS 213;ASP 362(Iron binding)
1uuwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 205;HIS 208 HIS 208;HIS 213;ASP 362(Iron binding)
1eg9A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 104 CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding)
1ndoA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 104 CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding)
1ndoC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 104 CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding)
1ndoE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 104 CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding)
1o7gA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 104 CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding)
1o7hA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 104 CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding)
1o7mA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 104 CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding)
1o7nA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 104 CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding)
1o7pA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 104 CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding)
1o7wA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 104 CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding)
1uuvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 104 CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding)
1uuwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 104 CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding)
1eg9B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ndoB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ndoD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ndoF Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1o7gB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1o7hB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1o7mB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1o7nB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1o7pB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1o7wB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1uuvB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1uuwB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
SCHEME I, p.30257-30260
[4]
p.575-582
[5]
p.11068-11070
[7]
Fig.1, p.1835-1836
[9]
Fig.2
[11]
Scheme 1, p.706-709
[14]
Scheme 2, p.1952
[17]
Fig.1, P.7065-7066
[18]
p.272-274
[19]
Fig.2
[20]
Fig
[21]
Scheme 2, Scheme 3, Fig.7, Fig.9, p.443-451
[22]

References
[1]
Resource
Comments
Medline ID
PubMed ID 7858982
Journal Bioorg Med Chem
Year 1994
Volume 2
Pages 727-34
Authors Whited GM, Downie JC, Hudlicky T, Fearnley SP, Dudding TC, Olivo HF, Parker D
Title Oxidation of 2-methoxynaphthalene by toluene, naphthalene and biphenyl dioxygenases:structure and absolute stereochemistry of metabolites.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8899998
Journal Appl Environ Microbiol
Year 1996
Volume 62
Pages 4073-80
Authors Resnick SM, Gibson DT
Title Regio- and stereospecific oxidation of fluorene, dibenzofuran, and dibenzothiophene by naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816-4.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 9374510
Journal J Biol Chem
Year 1997
Volume 272
Pages 30254-60
Authors Di Gennaro P, Sello G, Bianchi D, D'Amico P
Title Specificity of substrate recognition by Pseudomonas fluorescens N3 dioxygenase. The role of the oxidation potential and molecular geometry.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS)
Medline ID 98298434
PubMed ID 9634695
Journal Structure
Year 1998
Volume 6
Pages 571-86
Authors Kauppi B, Lee K, Carredano E, Parales RE, Gibson DT, Eklund H, Ramaswamy S
Title Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase.
Related PDB 1ndo
Related UniProtKB P0A110 P0A111 P23094 P23095
[5]
Resource
Comments
Medline ID
PubMed ID 10390817
Journal Appl Microbiol Biotechnol
Year 1999
Volume 51
Pages 592-7
Authors Barriault D, Sylvestre M
Title Functionality of biphenyl 2,3-dioxygenase components in naphthalene 1,2-dioxygenase.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 10460161
Journal Biochemistry
Year 1999
Volume 38
Pages 11062-72
Authors Coulter ED, Moon N, Batie CJ, Dunham WR, Ballou DP
Title Electron paramagnetic resonance measurements of the ferrous mononuclear site of phthalate dioxygenase substituted with alternate divalent metal ions: direct evidence for ligation of two histidines in the copper(II)-reconstituted protein.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10074076
Journal J Bacteriol
Year 1999
Volume 181
Pages 1831-7
Authors Parales RE, Parales JV, Gibson DT
Title Aspartate 205 in the catalytic domain of naphthalene dioxygenase is essential for activity.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 10713518
Journal Acta Crystallogr D Biol Crystallogr
Year 2000
Volume 56
Pages 313-21
Authors Carredano E, Kauppi B, Choudhury D, Ramaswamy S
Title Pseudo-symmetry characterization and refinement of a trigonal crystal form of naphthalene 1,2-dioxygenase.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 10692370
Journal J Bacteriol
Year 2000
Volume 182
Pages 1641-9
Authors Parales RE, Lee K, Resnick SM, Jiang H, Lessner DJ, Gibson DT
Title Substrate specificity of naphthalene dioxygenase: effect of specific amino acids at the active site of the enzyme.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 10986254
Journal J Bacteriol
Year 2000
Volume 182
Pages 5495-504
Authors Parales RE, Resnick SM, Yu CL, Boyd DR, Sharma ND, Gibson DT
Title Regioselectivity and enantioselectivity of naphthalene dioxygenase during arene cis-dihydroxylation: control by phenylalanine 352 in the alpha subunit.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10669618
Journal J Mol Biol
Year 2000
Volume 296
Pages 701-12
Authors Carredano E, Karlsson A, Kauppi B, Choudhury D, Parales RE, Parales JV, Lee K, Gibson DT, Eklund H, Ramaswamy S
Title Substrate binding site of naphthalene 1,2-dioxygenase: functional implications of indole binding.
Related PDB 1eg9
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 10919518
Journal Res Microbiol
Year 2000
Volume 151
Pages 383-91
Authors Gennaro PD, Galli E, Orsini F, Pelizzoni F, Sello G, Bestetti G
Title Development of biocatalysts carrying naphthalene dioxygenase and dihydrodiol dehydrogenase genes inducible in aerobic and anaerobic conditions.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11849939
Journal Curr Opin Biotechnol
Year 2001
Volume 12
Pages 564-73
Authors Boyd DR, Sharma ND, Allen CC
Title Aromatic dioxygenases: molecular biocatalysis and applications.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 11056161
Journal J Biol Chem
Year 2001
Volume 276
Pages 1945-53
Authors Wolfe MD, Parales JV, Gibson DT, Lipscomb JD
Title Single turnover chemistry and regulation of O2 activation by the oxygenase component of naphthalene 1,2-dioxygenase.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 11641767
Journal J Ind Microbiol Biotechnol
Year 2001
Volume 27
Pages 94-103
Authors Yu CL, Parales RE, Gibson DT
Title Multiple mutations at the active site of naphthalene dioxygenase affect regioselectivity and enantioselectivity.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 12189839
Journal Chem Commun (Camb)
Year 2002
Volume (14)
Pages 1452-3
Authors Boyd DR, Sharma ND, Kennedy MA, Shepherd SD, Malone JF, Alves-Areias A, Holt R, Allenmark SG, Lemurell MA, Dalton H, Luckarift H
Title Enzyme-catalysed oxygenation and deoxygenation routes to chiral thiosulfinates.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 12783560
Journal J Am Chem Soc
Year 2003
Volume 125
Pages 7056-66
Authors Yang TC, Wolfe MD, Neibergall MB, Mekmouche Y, Lipscomb JD, Hoffman BM
Title Substrate binding to NO-ferro-naphthalene 1,2-dioxygenase studied by high-resolution Q-band pulsed 2H-ENDOR spectroscopy.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 12695887
Journal J Ind Microbiol Biotechnol
Year 2003
Volume 30
Pages 271-8
Authors Parales RE
Title The role of active-site residues in naphthalene dioxygenase.
Related PDB
Related UniProtKB
[19]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12586937
Journal Science
Year 2003
Volume 299
Pages 1039-42
Authors Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S
Title Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron.
Related PDB 1ndo 1o7g 1o7h 1o7m 1o7n 1o7p 1o7w
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 12586930
Journal Science
Year 2003
Volume 299
Pages 1024-5
Authors Kovacs JA
Title Biochemistry. How iron activates O2.
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 15042436
Journal J Biol Inorg Chem
Year 2004
Volume 9
Pages 439-52
Authors Bassan A, Blomberg MR, Siegbahn PE
Title A theoretical study of the cis-dihydroxylation mechanism in naphthalene 1,2-dioxygenase.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 15942729
Journal J Biol Inorg Chem
Year 2005
Volume 10
Pages 483-9
Authors Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S
Title NO binding to naphthalene dioxygenase.
Related PDB 1uuv 1uuw
Related UniProtKB

Comments
This enzyme belongs to a large family of bacterial Rieske non-heme iron oxygenases. This enzyme is a part of naphthalene 1,2-dioxygenase system (NDOS).
Although NADH and NAD+ are included as a substrate and a product, respectively, they do not interact directly with this enzyme. According to the literature [4], [7], [14] and [18], the reaction proceeds as follows:
(#) Ferredoxin-NAD+ reductase (cf. D00071 in EzCatDB) of NDOS catalyzes electron transfer from NADH to Ferredoxin of NDOS.
(A) Electron transfer from Ferredoxin to the FE2S2 (Iron-sulfur) of the oxidized form of this enzyme.
(A1) Indirect transfer through Trp211 from the adjacent alpha-subunit and Val100, to Cys101, which is bound to FE2S2 (see [4]).
(B) Electron transfer from the FE2S2 to the mononuclear iron center of the adjacent subunit of this enzyme.
(B1) Indirect transfer through His104 bound to the FE2S2, the sidechain of Asp205 from the adjacent alpha-subunit, and His208 bound to the mononuclear iron center from the adjacent alpha-subunit (see [4] and [7]).
(C) Oxygenation of naphthalene at the mononuclear iron center.

Created Updated
2005-05-31 2018-04-23