DB code: S00031

CATH domain 1.10.630.10 : Cytochrome p450 Catalytic domain
E.C. 1.7.1.14
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.10.630.10 : Cytochrome p450 S00033 M00154 S00030

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P23295 Cytochrome P450 55A1
EC 1.14.-.-
CYPLVA1
P450 DNIR
Nitric oxide reductase
P450nor
PF00067 (p450)
[Graphical View]

KEGG enzyme name
nitric oxide reductase [NAD(P), nitrous oxide-forming]
fungal nitric oxide reductase
cytochrome P450nor
NOR (ambiguous)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P23295 NOR_FUSOX Nitrous oxide + NAD(P)(+) + H(2)O = 2 nitric oxide + NAD(P)H. Heme group.

KEGG Pathways
Map code Pathways E.C.
MAP00910 Nitrogen metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00032 C00533 C00004 C00005 C00080 C00887 C00003 C00006 C00001
E.C.
Compound Heme Nitric oxide NADH NADPH H+ Nitrous oxide NAD NADP+ H2O
Type aromatic ring (with nitrogen atoms),carboxyl group,heavy metal others amide group,amine group,nucleotide amide group,amine group,nucleotide others others amide group,amine group,nucleotide amide group,amine group,nucleotide H2O
ChEBI 17627
 26355
 17627
 26355
 		16480
 16480
 		16908
 16908
 		16474
 16474
 		15378
 15378
 		17045
 17045
 		15846
 15846
 		18009
 18009
 		15377
 15377
PubChem 145068
 145068
 		439153
 439153
 		5884
 5884
 		1038
 1038
 		948
 948
 		5893
 5893
 		5886
 5886
 		22247451
 962
 22247451
 962
1cl6A Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:HEM-_NO
1cmjA Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:HEM-_NO
1cmnA Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:HEM-_NO
1eheA Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ehfA Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ehgA Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1f24A Bound:HEM Bound:_NO Unbound Unbound Unbound Unbound Unbound Unbound
1f25A Bound:HEM Bound:_NO Unbound Unbound Unbound Unbound Unbound Unbound
1f26A Bound:HEM Bound:_NO Unbound Unbound Unbound Unbound Unbound Unbound
1gedA Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1geiA Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:HEM-NBN
1gejA Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:HEM-NBN
1jfbA Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1jfcA Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:HEM-CMO
1romA Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2romA Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:HEM-CMO
1ulwA Bound:HEM Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1xqdA Bound:HEM Unbound Unbound Unbound Unbound Analogue:DND Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [8], [9], [13], [14], [15]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1cl6A THR 243;SER 286;ASP 393 CYS 352(Heme iron binding)
1cmjA THR 243;;ASP 393 CYS 352(Heme iron binding) mutant S286T
1cmnA THR 243;;ASP 393 CYS 352(Heme iron binding) mutant S286V
1eheA THR 243;SER 286;ASP 393 CYS 352(Heme iron binding)
1ehfA THR 243;;ASP 393 CYS 352(Heme iron binding) mutant S286T
1ehgA THR 243;;ASP 393 CYS 352(Heme iron binding) mutant S286V
1f24A ;SER 286;ASP 393 CYS 352(Heme iron binding) mutant T243A
1f25A ;SER 286;ASP 393 CYS 352(Heme iron binding) mutant T243N
1f26A ;SER 286;ASP 393 CYS 352(Heme iron binding) mutant T243V
1gedA THR 243;SER 286;ASP 393 CYS 352(Heme iron binding)
1geiA THR 243;SER 286;ASP 393 CYS 352(Heme iron binding)
1gejA THR 243;SER 286;ASP 393 CYS 352(Heme iron binding)
1jfbA THR 243;SER 286;ASP 393 CYS 352(Heme iron binding)
1jfcA THR 243;SER 286;ASP 393 CYS 352(Heme iron binding)
1romA THR 243;SER 286;ASP 393 CYS 352(Heme iron binding)
2romA THR 243;SER 286;ASP 393 CYS 352(Heme iron binding)
1ulwA THR 243;SER 286;ASP 393 CYS 352(Heme iron binding)
1xqdA THR 243;SER 286;ASP 393 CYS 352(Heme iron binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.1622-1623
[5]
[7]
[9]
p.830-831
[10]
p.8845-8846
[11]
Fig.2, p.12965
[14]
p.4824-4825
[15]
p.107
[16]
[22]
Fig.2
[24]
p.212-214

References
[1]
Resource
Comments
Medline ID
PubMed ID 8196045
Journal J Mol Biol
Year 1994
Volume 239
Pages 158-9
Authors Nakahara K, Shoun H, Adachi S, Iizuka T, Shiro Y
Title Crystallization and preliminary X-ray diffraction studies of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 7619804
Journal Biochemistry
Year 1995
Volume 34
Pages 9052-8
Authors Shiro Y, Fujii M, Isogai Y, Adachi S, Iizuka T, Obayashi E, Makino R, Nakahara K, Shoun H
Title Iron-ligand structure and iron redox property of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum: relevance to its NO reduction activity.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 7829493
Journal J Biol Chem
Year 1995
Volume 270
Pages 1617-23
Authors Shiro Y, Fujii M, Iizuka T, Adachi S, Tsukamoto K, Nakahara K, Shoun H
Title Spectroscopic and kinetic studies on reaction of cytochrome P450nor with nitric oxide. Implication for its nitric oxide reduction mechanism.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 9010609
Journal Biochimie
Year 1996
Volume 78
Pages 792-9
Authors Kudo T, Tomura D, Liu DL, Dai XQ, Shoun H
Title Two isozymes of P450nor of Cylindrocarpon tonkinense: molecular cloning of the cDNAs and genes, expressions in the yeast, and the putative NAD(P)H-binding site.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID
Journal J Biol Inorg Chem
Year 1996
Volume 1
Pages 372-6
Authors Rietjens IM, Osman AM, Veeger C, Zakharieva O, Antony J, Grodzicki M, Trautwein AX
Title On the role of the axial ligand in heme-based catalysis of the peroxidase and P450 type.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 9003438
Journal Biochim Biophys Acta
Year 1997
Volume 1337
Pages 66-74
Authors Imai Y, Okamoto N, Nakahara K, Shoun H
Title Absorption spectral studies on heme ligand interactions of P-450nor.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 9074619
Journal Biochim Biophys Acta
Year 1997
Volume 1338
Pages 93-9
Authors Toritsuka N, Shoun H, Singh UP, Park SY, Iizuka T, Shiro Y
Title Functional and structural comparison of nitric oxide reductases from denitrifying fungi Cylindrocarpon tonkinense and Fusarium oxysporum.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 9256249
Journal FEBS Lett
Year 1997
Volume 412
Pages 346-50
Authors Park SY, Shimizu H, Adachi S, Shiro Y, Iizuka T, Nakagawa A, Tanaka I, Shoun H, Hori H
Title Crystallization, preliminary diffraction and electron paramagnetic resonance studies of a single crystal of cytochrome P450nor.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID 97475224
PubMed ID 9334748
Journal Nat Struct Biol
Year 1997
Volume 4
Pages 827-32
Authors Park SY, Shimizu H, Adachi S, Nakagawa A, Tanaka I, Nakahara K, Shoun H, Obayashi E, Nakamura H, Iizuka T, Shiro Y
Title Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum.
Related PDB 1rom 2rom
Related UniProtKB P23295
[10]
Resource
Comments
Medline ID
PubMed ID 9636024
Journal Biochemistry
Year 1998
Volume 37
Pages 8839-47
Authors Okamoto N, Imai Y, Shoun H, Shiro Y
Title Site-directed mutagenesis of the conserved threonine (Thr243) of the distal helix of fungal cytochrome P450nor.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID
Journal J Am Chem Soc
Year 1998
Volume 120
Pages 12964-65
Authors Obayashi E, Takahashi S, Shiro Y
Title Electronic structure of reaction intermediate of cytochrome P450nor in its nitric oxide reduction.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 10369184
Journal Nitric Oxide
Year 1999
Volume 3
Pages 142-52
Authors Mehl M, Daiber A, Herold S, Shoun H, Ullrich V
Title Peroxynitrite reaction with heme proteins.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11004439
Journal Biochim Biophys Acta
Year 2000
Volume 1459
Pages 266-73
Authors Hendriks J, Oubrie A, Castresana J, Urbani A, Gemeinhardt S, Saraste M
Title Nitric oxide reductases in bacteria.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS)
Medline ID 20138220
PubMed ID 10671516
Journal J Biol Chem
Year 2000
Volume 275
Pages 4816-26
Authors Shimizu H, Obayashi E, Gomi Y, Arakawa H, Park SY, Nakamura H, Adachi S, Shoun H, Shiro Y
Title Proton delivery in NO reduction by fungal nitric-oxide reductase. Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes.
Related PDB 1cl6 1cmj 1cmn
Related UniProtKB P23295
[15]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11132616
Journal J Inorg Biochem
Year 2000
Volume 82
Pages 103-11
Authors Obayashi E, Shimizu H, Park SY, Shoun H, Shiro Y
Title Mutation effects of a conserved threonine (Thr243) of cytochrome P450nor on its structure and function.
Related PDB 1f24 1f25 1f26
Related UniProtKB
[16]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11051564
Journal J Inorg Biochem
Year 2000
Volume 81
Pages 191-205
Authors Shimizu H, Park S, Lee D, Shoun H, Shiro Y
Title Crystal structures of cytochrome P450nor and its mutants (Ser286-->Val, Thr) in the ferric resting state at cryogenic temperature: a comparative analysis with monooxygenase cytochrome P450s.
Related PDB 1ehe 1ehf 1ehg
Related UniProtKB
[17]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS)
Medline ID 21159060
PubMed ID 11258878
Journal Biochemistry
Year 2001
Volume 40
Pages 2669-77
Authors Lee DS, Park SY, Yamane K, Obayashi E, Hori H, Shiro Y
Title Structural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam.
Related PDB 1gei 1gej
Related UniProtKB P23295
[18]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11076941
Journal J Biol Chem
Year 2001
Volume 276
Pages 5020-6
Authors Kudo T, Takaya N, Park SY, Shiro Y, Shoun H
Title A positively charged cluster formed in the heme-distal pocket of cytochrome P450nor is essential for interaction with NADH.
Related PDB 1ged
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 11346959
Journal Planta
Year 2001
Volume 212
Pages 835-41
Authors Stohr C, Strube F, Marx G, Ullrich WR, Rockel P
Title A plasma membrane-bound enzyme of tobacco roots catalyses the formation of nitric oxide from nitrite.
Related PDB
Related UniProtKB
[20]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS)
Medline ID 21620774
PubMed ID 11752781
Journal Acta Crystallogr D Biol Crystallogr
Year 2002
Volume 58
Pages 81-9
Authors Shimizu H, Park SY, Shiro Y, Adachi S
Title X-ray structure of nitric oxide reductase (cytochrome P450nor) at atomic resolution.
Related PDB 1jfb 1jfc
Related UniProtKB P23295
[21]
Resource
Comments
Medline ID
PubMed ID 12105197
Journal J Biol Chem
Year 2002
Volume 277
Pages 33842-7
Authors Zhang L, Kudo T, Takaya N, Shoun H
Title The B' helix determines cytochrome P450nor specificity for the electron donors NADH and NADPH.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID
Journal J Mol Struct Theochem
Year 2003
Volume 624
Pages 309-22
Authors Tsukamoto K, Nakamura S, Shimizu K
Title SAM1 semiempirical calculations on the catalytic cycle of nitric oxide reductase from Fusarium oxysporum.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 14766741
Journal J Biol Chem
Year 2004
Volume 279
Pages 17120-5
Authors Gronberg KL, Watmough NJ, Thomson AJ, Richardson DJ, Field SJ
Title Redox-dependent open and closed forms of the active site of the bacterial respiratory nitric-oxide reductase revealed by cyanide binding studies.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 15313618
Journal J Mol Biol
Year 2004
Volume 342
Pages 207-17
Authors Oshima R, Fushinobu S, Su F, Zhang L, Takaya N, Shoun H
Title Structural evidence for direct hydride transfer from NADH to cytochrome P450nor.
Related PDB 1ulw 1xqd
Related UniProtKB

Comments
Although Swissprot data, P23295, reports that E.C. number of this enzyme is 1.14.-.-, it has been transferred to 1.7.1.14.
NAD is used as an "acceptor", whilst NADH is used as a "reduced acceptor" in this enzyme.
This enzyme catalyzes three successive reactions as follows (see [18]; These reactions are irreversible.):
(A) Fe3+ + NO -> Fe3+-NO
(B) Fe3+-NO + NADH -> Intermediate + NAD+
(C) Intermediate + NO + H+ -> Fe3+ + N2O +H2O

Created Updated
2004-05-17 2012-10-03