EzCatDB: M00154

DB codeM00154
CATH domainDomain 11.10.630.10Catalytic domain
Domain 23.40.50.360
Domain 3-.-.-.-
Domain 4-.-.-.-
E.C.1.14.14.1,1.6.2.4

CATH domainRelated DB codes (homologues)
1.10.630.10S00033,S00031,S00030
3.40.50.360S00522,S00343,M00006

Enzyme Name
Swiss-protKEGG

P14779
Protein nameBifunctional P-450/NADPH-P450 reductaseunspecific monooxygenase
   (EC 1.14.14.1)
microsomal monooxygenase
   (EC 1.14.14.1)
xenobiotic monooxygenase
   (EC 1.14.14.1)
aryl-4-monooxygenase
   (EC 1.14.14.1)
aryl hydrocarbon hydroxylase
   (EC 1.14.14.1)
microsomal P-450
   (EC 1.14.14.1)
flavoprotein-linked monooxygenase
   (EC 1.14.14.1)
flavoprotein monooxygenase
   (EC 1.14.14.1)
NADPH---hemoprotein reductase
   (EC 1.6.2.4)
CPR
   (EC 1.6.2.4)
FAD-cytochrome c reductase
   (EC 1.6.2.4)
NADP---cytochrome c reductase
   (EC 1.6.2.4)
NADP---cytochrome reductase
   (EC 1.6.2.4)
NADPH-dependent cytochrome c reductase
   (EC 1.6.2.4)
NADPH:P-450 reductase
   (EC 1.6.2.4)
NADPH:ferrihemoprotein oxidoreductase
   (EC 1.6.2.4)
NADPH---cytochrome P-450 oxidoreductase
   (EC 1.6.2.4)
NADPH---cytochrome c oxidoreductase
   (EC 1.6.2.4)
NADPH---cytochrome c reductase
   (EC 1.6.2.4)
NADPH---cytochrome p-450 reductase
   (EC 1.6.2.4)
NADPH---ferricytochrome c oxidoreductase
   (EC 1.6.2.4)
NADPH---ferrihemoprotein reductase
   (EC 1.6.2.4)
TPNH2 cytochrome c reductase
   (EC 1.6.2.4)
TPNH-cytochrome c reductase
   (EC 1.6.2.4)
aldehyde reductase (NADPH-dependent)
   (EC 1.6.2.4)
cytochrome P-450 reductase
   (EC 1.6.2.4)
cytochrome c reductase (reduced nicotinamide adenine dinucleotidephosphate, NADPH, NADPH-dependent)
   (EC 1.6.2.4)
dihydroxynicotinamide adenine dinucleotide phosphate-cytochrome creductase
   (EC 1.6.2.4)
ferrihemoprotein P-450 reductase
   (EC 1.6.2.4)
reduced nicotinamide adenine dinucleotide phosphate-cytochrome creductase
   (EC 1.6.2.4)
reductase, cytochrome c (reduced nicotinamide adenine dinucleotidephosphate)
   (EC 1.6.2.4)
SynonymsCytochrome P450(BM-3)
P450BM-3
IncludesCytochrome P450 102
   EC 1.14.14.1
NADPH--cytochrome P450 reductase
   EC 1.6.2.4

KEGG pathways
MAP codePathwaysE.C.
MAP00071Fatty acid metabolism1.14.14.1
MAP00150Androgen and estrogen metabolism1.14.14.1
MAP00232Caffeine metabolism1.14.14.1
MAP00361gamma-Hexachlorocyclohexane degradation1.14.14.1
MAP00380Tryptophan metabolism1.14.14.1
MAP00590Arachidonic acid metabolism1.14.14.1
MAP00591Linoleic acid metabolism1.14.14.1
MAP00830Retinol metabolism1.14.14.1
MAP00980Metabolism of xenobiotics by cytochrome P4501.14.14.1
MAP00982Drug metabolism - cytochrome P4501.14.14.1
MAP00983Drug metabolism - other enzymes1.14.14.1

Swiss-prot:Accession NumberP14779
Entry nameCPXB_BACME
ActivityNADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein.,RH + reduced flavoprotein + O(2) = ROH + oxidized flavoprotein + H(2)O.
Subunit
Subcellular locationCytoplasm (By similarity).
CofactorFAD.,FMN.,Heme group.


CofactorsSubstratesProducts
KEGG-idC00032C00061C00016C03024C00007C01371C00162C01598C06604C00005C00080C99999C00923C03161C00001C01335C05102C05643C06606C00283C00006C99999C00924
E.C.1.14.14.11.6.2.41.6.2.41.14.14.11.14.14.11.14.14.11.14.14.11.14.14.11.14.14.11.6.2.41.6.2.41.6.2.41.6.2.41.14.14.11.14.14.11.14.14.11.14.14.11.14.14.11.14.14.11.14.14.11.6.2.41.6.2.41.6.2.4
CompoundHemeFMNFADReduced flavoproteinO2RHFatty acidMelatoninParathionNADPHH+Oxidized hemoproteinFerricytochromeOxidized flavoproteinH2OROHalpha-Hydroxy fatty acid6-HydroxymelatoninParaoxonHydrogen sulfideNADP+Reduced hemoproteinFerrocytochrome
Typearomatic ring (with nitrogen atoms),carboxyl group,heavy metalamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ionamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotideamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),peptide/proteinotherslipidfatty acidamide group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms)aromatic ring (only carbon atom),nitro group,phosphate group/phosphate ion,sulfide groupamide group,amine group,nucleotideothersaromatic ring (with nitrogen atoms),carboxyl group,heavy metal,peptide/proteinaromatic ring (with nitrogen atoms),carboxyl group,heavy metalamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),peptide/proteinH2Olipidcarbohydrate,fatty acidamide group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms)aromatic ring (only carbon atom),nitro group,phosphate group/phosphate ionsulfhydryl groupamide group,amine group,nucleotidearomatic ring (with nitrogen atoms),carboxyl group,heavy metal,peptide/proteinaromatic ring (with nitrogen atoms),carboxyl group,heavy metal
1bu7ABound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bu7BBound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bvyAAnalogue:HEM-EDOUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
Bound:EDO 1003UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bvyBAnalogue:HEM-EDOUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
Bound:EDO 1004UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1fagABound:HEMUnboundUnboundUnboundUnboundUnboundBound:PAMUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1fagBBound:HEMUnboundUnboundUnboundUnboundUnboundBound:PAMUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1fagCBound:HEMUnboundUnboundUnboundUnboundUnboundBound:PAMUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1fagDBound:HEMUnboundUnboundUnboundUnboundUnboundBound:PAMUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1fahAAnalogue:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1fahBAnalogue:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jmeABound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jmeBBound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jpzABound:HEMUnboundUnboundUnboundUnboundUnboundAnalogue:140UnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1jpzBBound:HEMUnboundUnboundUnboundUnboundUnboundAnalogue:140UnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1p0vABound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1p0vBBound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1p0wABound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1p0wBBound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1p0xABound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1p0xBBound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2bmhABound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2bmhBBound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2hpdABound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2hpdBBound:HEMUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1bvyFUnboundBound:FMNUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
Analogue:HEM-EDO(chain A)UnboundUnbound
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P00179 & literature [11], [34]
pdbCatalytic residuesCofactor-binding residuescomment
1bu7ATHR 268
CYS 400(Heme iron binding)

1bu7BTHR 268
CYS 400(Heme iron binding)

1bvyATHR 268
CYS 400(Heme iron binding)

1bvyBTHR 268
CYS 400(Heme iron binding)

1fagATHR 268
CYS 400(Heme iron binding)

1fagBTHR 268
CYS 400(Heme iron binding)

1fagCTHR 268
CYS 400(Heme iron binding)

1fagDTHR 268
CYS 400(Heme iron binding)

1fahA       
CYS 400(Heme iron binding)
mutant T268A
1fahB       
CYS 400(Heme iron binding)
mutant T268A
1jmeATHR 268
CYS 400(Heme iron binding)
mutant F393H
1jmeBTHR 268
CYS 400(Heme iron binding)
mutant F393H
1jpzATHR 268
CYS 400(Heme iron binding)

1jpzBTHR 268
CYS 400(Heme iron binding)

1p0vATHR 268
CYS 400(Heme iron binding)
mutant F393A
1p0vBTHR 268
CYS 400(Heme iron binding)
mutant F393A
1p0wATHR 268
CYS 400(Heme iron binding)
mutant F393W
1p0wBTHR 268
CYS 400(Heme iron binding)
mutant F393W
1p0xATHR 268
CYS 400(Heme iron binding)
mutant F393Y
1p0xBTHR 268
CYS 400(Heme iron binding)
mutant F393Y
2bmhATHR 268
CYS 400(Heme iron binding)

2bmhBTHR 268
CYS 400(Heme iron binding)

2hpdATHR 268
CYS 400(Heme iron binding)

2hpdBTHR 268
CYS 400(Heme iron binding)

1bvyF



References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[11]Fig.4, p.14737-147399
[16]Fig.1, p.414
[17]Fig.5, Fig.6, p.13820-13822
[18]

[20]p.143-145
[21]Fig.9, p.8408-8412
[27]

[29]Fig.5, p.1867
[34]p.13463-13464
[39]


references
[1]
CommentsCHARACTERIZATION
Medline ID92088245
PubMed ID1727637
JournalArch Biochem Biophys
Year1992
Volume292
Pages20-8
AuthorsBoddupalli SS, Pramanik BC, Slaughter CA, Estabrook RW, Peterson JA
TitleFatty acid monooxygenation by P450BM-3: product identification and proposed mechanisms for the sequential hydroxylation reactions.
Related Swiss-protP14779
[2]
PubMed ID1334408
JournalBiochem J
Year1992
Volume288
Pages503-9
AuthorsMiles JS, Munro AW, Rospendowski BN, Smith WE, McKnight J, Thomson AJ
TitleDomains of the catalytically self-sufficient cytochrome P-450 BM-3. Genetic construction, overexpression, purification and spectroscopic characterization.
[3]
PubMed ID1544935
JournalJ Biol Chem
Year1992
Volume267
Pages5614-20
AuthorsTuck SF, Peterson JA, Ortiz de Montellano PR
TitleActive site topologies of bacterial cytochromes P450101 (P450cam), P450108 (P450terp), and P450102 (P450BM-3). In situ rearrangement of their phenyl-iron complexes.
[4]
PubMed ID1608967
JournalProc Natl Acad Sci U S A
Year1992
Volume89
Pages5567-71
AuthorsBoddupalli SS, Hasemann CA, Ravichandran KG, Lu JY, Goldsmith EJ, Deisenhofer J, Peterson JA
TitleCrystallization and preliminary x-ray diffraction analysis of P450terp and the hemoprotein domain of P450BM-3, enzymes belonging to two distinct classes of the cytochrome P450 superfamily.
[5]
PubMed ID8257708
JournalBiochemistry
Year1993
Volume32
Pages13732-41
AuthorsShirane N, Sui Z, Peterson JA, Ortiz de Montellano PR
TitleCytochrome P450BM-3 (CYP102): regiospecificity of oxidation of omega-unsaturated fatty acids and mechanism-based inactivation.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-471
Medline ID93342510
PubMed ID8342039
JournalScience
Year1993
Volume261
Pages731-6
AuthorsRavichandran KG, Boddupalli SS, Hasermann CA, Peterson JA, Deisenhofer J
TitleCrystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's.
Related PDB2hpd
Related Swiss-protP14779
[7]
PubMed ID8463285
JournalJ Biol Chem
Year1993
Volume268
Pages7553-61
AuthorsKlein ML, Fulco AJ
TitleCritical residues involved in FMN binding and catalytic activity in cytochrome P450BM-3.
[8]
PubMed ID7980400
JournalBiochem J
Year1994
Volume303
Pages423-8
AuthorsMunro AW, Malarkey K, McKnight J, Thomson AJ, Kelly SM, Price NC, Lindsay JG, Coggins JR, Miles JS
TitleThe role of tryptophan 97 of cytochrome P450 BM3 from Bacillus megaterium in catalytic function. Evidence against the 'covalent switching' hypothesis of P-450 electron transfer.
[9]
PubMed ID7700866
JournalProtein Eng
Year1994
Volume7
Pages1345-51
AuthorsRuan KH, Milfeld K, Kulmacz RJ, Wu KK
TitleComparison of the construction of a 3-D model for human thromboxane synthase using P450cam and BM-3 as templates: implications for the substrate binding pocket.
[10]
CommentsX-ray crystallography
JournalActa Crystallogr D Biol Crystallogr
Year1995
Volume51
Pages21-32
AuthorsLi H., Poulos TL
TitleA method for processing diffraction data from twinned protein crystals and its application in the structure determination of an FAD/NADH-binding fragment of nitrate reductase.
Related PDB2bmh
[11]
CommentsX-ray crystallography
PubMed ID7578081
JournalBiochemistry
Year1995
Volume34
Pages14733-40
AuthorsYeom H, Sligar SG, Li H, Poulos TL, Fulco AJ
TitleThe role of Thr268 in oxygen activation of cytochrome P450BM-3.
Related PDB1fah
[12]
PubMed ID7578214
JournalBiochim Biophys Acta
Year1995
Volume1231
Pages255-64
AuthorsMunro AW, Lindsay JG, Coggins JR, Kelly SM, Price NC
TitleNADPH oxidase activity of cytochrome P-450 BM3 and its constituent reductase domain.
[13]
PubMed ID8829615
JournalBiochem Mol Biol Int
Year1996
Volume38
Pages553-8
AuthorsUvarov VYu, Lyashenko AA, Zimin AG
TitleComparative analysis of the secondary structural motifs of P450BM-3 and the regions located upstream of the calmodulin-binding domain in the nitric oxide synthases.
[14]
PubMed ID8942669
JournalBiochemistry
Year1996
Volume35
Pages15029-37
AuthorsMurataliev MB, Feyereisen R
TitleFunctional interactions in cytochrome P450BM3. Fatty acid substrate binding alters electron-transfer properties of the flavoprotein domain.
[15]
PubMed ID9010597
JournalBiochimie
Year1996
Volume78
Pages695-9
AuthorsLi H, Poulos TL
TitleConformational dynamics in cytochrome P450-substrate interactions.
[16]
PubMed ID8612070
JournalNat Struct Biol
Year1996
Volume3
Pages414-7
AuthorsModi S, Sutcliffe MJ, Primrose WU, Lian LY, Roberts GC
TitleThe catalytic mechanism of cytochrome P450 BM3 involves a 6 A movement of the bound substrate on reduction.
[17]
PubMed ID9374858
JournalBiochemistry
Year1997
Volume36
Pages13816-23
AuthorsDaff SN, Chapman SK, Turner KL, Holt RA, Govindaraj S, Poulos TL, Munro AW
TitleRedox control of the catalytic cycle of flavocytochrome P-450 BM3.
[18]
PubMed ID9048540
JournalBiochemistry
Year1997
Volume36
Pages1567-72
AuthorsOliver CF, Modi S, Sutcliffe MJ, Primrose WU, Lian LY, Roberts GC
TitleA single mutation in cytochrome P450 BM3 changes substrate orientation in a catalytic intermediate and the regiospecificity of hydroxylation.
[19]
PubMed ID9284282
JournalBiophys J
Year1997
Volume73
Pages1147-59
AuthorsArnold GE, Ornstein RL
TitleMolecular dynamics study of time-correlated protein domain motions and molecular flexibility: cytochrome P450BM-3.
[20]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-471
Medline ID97185914
PubMed ID9033595
JournalNat Struct Biol
Year1997
Volume4
Pages140-6
AuthorsLi H, Poulos TL
TitleThe structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid.
Related PDB1fag
Related Swiss-protP14779
[21]
PubMed ID9204888
JournalBiochemistry
Year1997
Volume36
Pages8401-12
AuthorsMurataliev MB, Klein M, Fulco A, Feyereisen R
TitleFunctional interactions in cytochrome P450BM3: flavin semiquinone intermediates, role of NADP(H), and mechanism of electron transfer by the flavoprotein domain.
[22]
PubMed ID9500975
JournalBiochem Biophys Res Commun
Year1998
Volume243
Pages811-5
AuthorsHudeeek J, Baumruk V, Anzenbacher P, Munro AW
TitleCatalytically self-sufficient P450 CYP102 (cytochrome P450 BM-3): resonance Raman spectral characterization of the heme domain and of the holoenzyme.
[23]
PubMed ID9843385
JournalBiochemistry
Year1998
Volume37
Pages15799-807
AuthorsNoble MA, Quaroni L, Chumanov GD, Turner KL, Chapman SK, Hanzlik RP, Munro AW
TitleImidazolyl carboxylic acids as mechanistic probes of flavocytochrome P-450 BM3.
[24]
PubMed ID10222011
JournalAnal Biochem
Year1999
Volume269
Pages359-66
AuthorsSchwaneberg U, Schmidt-Dannert C, Schmitt J, Schmid RD
TitleA continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A.
[25]
PubMed ID9888815
JournalBiochemistry
Year1999
Volume38
Pages751-61
AuthorsDavydov DR, Hui Bon Hoa G, Peterson JA
TitleDynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: comparison with P450cam and P450 2B4.
[26]
PubMed ID10521277
JournalBiochemistry
Year1999
Volume38
Pages13699-706
AuthorsDeng TJ, Proniewicz LM, Kincaid JR, Yeom H, Macdonald ID, Sligar SG
TitleResonance Raman studies of cytochrome P450BM3 and its complexes with exogenous ligands.
[27]
PubMed ID10593892
JournalJ Biol Chem
Year1999
Volume274
Pages36097-106
AuthorsSevrioukova IF, Hazzard JT, Tollin G, Poulos TL
TitleThe FMN to heme electron transfer in cytochrome P450BM-3. Effect of chemical modification of cysteines engineered at the FMN-heme domain interaction site.
[28]
PubMed ID10447203
JournalJ Biomol Struct Dyn
Year1999
Volume16
Pages1189-203
AuthorsChang YT, Loew GH
TitleMolecular dynamics simulations of P450 BM3--examination of substrate-induced conformational change.
[29]
CommentsX-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-458 AND 459-649
Medline ID99162523
PubMed ID10051560
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages1863-8
AuthorsSevrioukova IF, Li H, Zhang H, Peterson JA, Poulos TL
TitleStructure of a cytochrome P450-redox partner electron-transfer complex.
Related PDB1bu7,1bvy
Related Swiss-protP14779
[30]
PubMed ID11164266
JournalJ Biotechnol
Year2000
Volume84
Pages249-57
AuthorsSchwaneberg U, Appel D, Schmitt J, Schmid RD
TitleP450 in biotechnology: zinc driven omega-hydroxylation of p-nitrophenoxydodecanoic acid using P450 BM-3 F87A as a catalyst.
[31]
PubMed ID10924137
JournalBiochemistry
Year2000
Volume39
Pages9419-29
AuthorsHaines DC, Sevrioukova IF, Peterson JA
TitleThe FMN-binding domain of cytochrome P450BM-3: resolution, reconstitution, and flavin analogue substitution.
[32]
PubMed ID11027150
JournalBiochemistry
Year2000
Volume39
Pages12699-707
AuthorsMurataliev MB, Feyereisen R
TitleFunctional interactions in cytochrome P450BM3. Evidence that NADP(H) binding controls redox potentials of the flavin cofactors.
[33]
PubMed ID11368173
JournalArch Biochem Biophys
Year2001
Volume387
Pages117-24
AuthorsCowart LA, Falck JR, Capdevila JH
TitleStructural determinants of active site binding affinity and metabolism by cytochrome P450 BM-3.
[34]
CommentsX-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-470
Medline ID21552924
PubMed ID11695892
JournalBiochemistry
Year2001
Volume40
Pages13456-65
AuthorsHaines DC, Tomchick DR, Machius M, Peterson JA
TitlePivotal role of water in the mechanism of P450BM-3.
Related PDB1jpz
Related Swiss-protP14779
[35]
CommentsX-ray crystallography
PubMed ID11695889
JournalBiochemistry
Year2001
Volume40
Pages13430-8
AuthorsOst TW, Munro AW, Mowat CG, Taylor PR, Pesseguiero A, Fulco AJ, Cho AK, Cheesman MA, Walkinshaw MD, Chapman SK
TitleStructural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3.
Related PDB1jme
[36]
PubMed ID12427012
JournalBiochemistry
Year2002
Volume41
Pages13514-25
AuthorsKariakin A, Davydov D, Peterson JA, Jung C
TitleA new approach to the study of protein-protein interaction by FTIR: complex formation between cytochrome P450BM-3 heme domain and FMN reductase domain.
[37]
PubMed ID12020135
JournalBioorg Chem
Year2002
Volume30
Pages107-18
AuthorsRock DA, Boitano AE, Wahlstrom JL, Rock DA, Jones JP
TitleUse of kinetic isotope effects to delineate the role of phenylalanine 87 in P450(BM-3).
[38]
PubMed ID12237219
JournalJ Inorg Biochem
Year2002
Volume91
Pages515-26
AuthorsFuziwara S, Sagami I, Rozhkova E, Craig D, Noble MA, Munro AW, Chapman SK, Shimizu T
TitleCatalytically functional flavocytochrome chimeras of P450 BM3 and nitric oxide synthase.
[39]
CommentsX-ray crystallography
PubMed ID14653735
JournalJ Am Chem Soc
Year2003
Volume125
Pages15010-20
AuthorsOst TW, Clark J, Mowat CG, Miles CS, Walkinshaw MD, Reid GA, Chapman SK, Daff S
TitleOxygen activation and electron transfer in flavocytochrome P450 BM3.
Related PDB1p0v,1p0w,1p0x

comments
This protein is composed of two enzymatic domain, the N-terminal doman of cytochrome P450 BM-3 (EC 1.14.14.1) and the C-terminal domain of NADPH-cytochrome-P450 reductase (EC 1.6.2.4).
The C-terminal NADPH-cytochrome-P450 reductase comprises flavodoxin-like domain, FAD-binding domain.
Whilst the N-terminal structure of cytochrome P450 BM-3 domain has been determined, the C-terminal enzyme structure is only partially determined (only flavodoxin-like domain; PDB 1bvy).
This enzyme catalyzes the following reactions (see [17] and [21]):
(A) Hydride transfer from NADPH to FAD, giving NADP+ and FADH2:
(B) Hydride transfer from FADH2 to FMN, giving FAD and FMNH2:
(C) Electron transfer from FMNH2 to P450 (or heme):
(D) Oxygenation of substrate by O2, producing hydroxylated product and water (H2O) at P450:

createdupdated
2004-10-202009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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