spacer
spacer

PDBsum entry 1oxa

Go to PDB code: 
protein ligands links
Oxidoreductase (oxygenase) PDB id
1oxa
Jmol
Contents
Protein chain
403 a.a. *
Ligands
HEM
DEB
Waters ×241
* Residue conservation analysis
PDB id:
1oxa
Name: Oxidoreductase (oxygenase)
Title: Cytochrome p450 (donor:o2 oxidoreductase)
Structure: Cytochrome p450 eryf. Chain: a
Source: Saccharopolyspora erythraea. Organism_taxid: 1836
Resolution:
2.10Å     R-factor:   0.196    
Authors: J.R.Cupp-Vickery,T.L.Poulos
Key ref: J.R.Cupp-Vickery and T.L.Poulos (1995). Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nat Struct Biol, 2, 144-153. PubMed id: 7749919
Date:
14-Jul-95     Release date:   07-Dec-95    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q00441  (CPXJ_SACEN) -  6-deoxyerythronolide B hydroxylase
Seq:
Struc:
404 a.a.
403 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 8 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     oxidoreductase activity     6 terms  

 

 
Nat Struct Biol 2:144-153 (1995)
PubMed id: 7749919  
 
 
Structure of cytochrome P450eryF involved in erythromycin biosynthesis.
J.R.Cupp-Vickery, T.L.Poulos.
 
  ABSTRACT  
 
Cytochrome P450eryF catalyzes the 6S-hydroxylation of 6-deoxyerythronolide B, the initial reaction in a multistep pathway to convert 6-deoxyerythronolide B into the antibiotic, erythromycin. The overall structure of P450eryF is similar to that of P450cam but differs in the exact positioning of several alpha-helices. The largest difference occurs in the B' helix and results in the enlargement of the substrate-binding pocket of P450eryF. The substrate is positioned with the macrolide ring perpendicular to the haem plane and contacts seven hydrophobic residues and three solvent molecules. The substrate participates in a network of hydrogen bonds that may provide a proton shuttle pathway in the oxygen cleavage reaction.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20121095 C.T.Walsh, and M.A.Fischbach (2010).
Natural products version 2.0: connecting genes to molecules.
  J Am Chem Soc, 132, 2469-2493.  
19808095 D.Ghosh, J.Griswold, M.Erman, and W.Pangborn (2010).
X-ray structure of human aromatase reveals an androgen-specific active site.
  J Steroid Biochem Mol Biol, 118, 197-202.  
20299274 F.O.Robert, J.Pandhal, and P.C.Wright (2010).
Exploiting cyanobacterial P450 pathways.
  Curr Opin Microbiol, 13, 301-306.  
20697922 O.Shoji, T.Fujishiro, S.Nagano, S.Tanaka, T.Hirose, Y.Shiro, and Y.Watanabe (2010).
Understanding substrate misrecognition of hydrogen peroxide dependent cytochrome P450 from Bacillus subtilis.
  J Biol Inorg Chem, 15, 1331-1339.
PDB codes: 2zqj 2zqx
20446763 T.C.Pochapsky, S.Kazanis, and M.Dang (2010).
Conformational plasticity and structure/function relationships in cytochromes P450.
  Antioxid Redox Signal, 13, 1273-1296.  
19179341 A.Nayeem, S.J.Chiang, S.W.Liu, Y.Sun, L.You, and J.Basch (2009).
Engineering enzymes for improved catalytic efficiency: a computational study of site mutagenesis in epothilone-B hydroxylase.
  Protein Eng Des Sel, 22, 257-266.  
19625248 C.Savino, L.C.Montemiglio, G.Sciara, A.E.Miele, S.G.Kendrew, P.Jemth, S.Gianni, and B.Vallone (2009).
Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate.
  J Biol Chem, 284, 29170-29179.
PDB codes: 2jjn 2jjo 2wio
19555717 I.G.Denisov, D.J.Frank, and S.G.Sligar (2009).
Cooperative properties of cytochromes P450.
  Pharmacol Ther, 124, 151-167.  
19389622 K.S.Ryan, and C.L.Drennan (2009).
Divergent pathways in the biosynthesis of bisindole natural products.
  Chem Biol, 16, 351-364.  
19074393 L.H.Xu, S.Fushinobu, H.Ikeda, T.Wakagi, and H.Shoun (2009).
Crystal structures of cytochrome P450 105P1 from Streptomyces avermitilis: conformational flexibility and histidine ligation state.
  J Bacteriol, 191, 1211-1219.
PDB codes: 3e5j 3e5k 3e5l
  19342783 Y.Yasutake, Y.Fujii, W.K.Cheon, A.Arisawa, and T.Tamura (2009).
Crystallization and preliminary X-ray diffraction studies of vitamin D3 hydroxylase, a novel cytochrome P450 isolated from Pseudonocardia autotrophica.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 372-375.  
18359283 D.Kim, Y.S.Heo, and P.R.Ortiz de Montellano (2008).
Efficient catalytic turnover of cytochrome P450(cam) is supported by a T252N mutation.
  Arch Biochem Biophys, 474, 150-156.  
18622598 E.M.Isin, and F.P.Guengerich (2008).
Substrate binding to cytochromes P450.
  Anal Bioanal Chem, 392, 1019-1030.  
18787124 L.Li, Z.Chang, Z.Pan, Z.Q.Fu, and X.Wang (2008).
Modes of heme binding and substrate access for cytochrome P450 CYP74A revealed by crystal structures of allene oxide synthase.
  Proc Natl Acad Sci U S A, 105, 13883-13888.
PDB codes: 3dam 3dan 3dbm
18838690 M.J.Cryle, and I.Schlichting (2008).
Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.
  Proc Natl Acad Sci U S A, 105, 15696-15701.
PDB codes: 3ejb 3ejd 3eje
18481342 M.Lisurek, B.Simgen, I.Antes, and R.Bernhardt (2008).
Theoretical and experimental evaluation of a CYP106A2 low homology model and production of mutants with changed activity and selectivity of hydroxylation.
  Chembiochem, 9, 1439-1449.  
17786430 C.Berne, D.Pignol, J.Lavergne, and D.Garcia (2007).
CYP201A2, a cytochrome P450 from Rhodopseudomonas palustris, plays a key role in the biodegradation of tributyl phosphate.
  Appl Microbiol Biotechnol, 77, 135-144.  
17273868 L.Li, H.Cheng, J.Gai, and D.Yu (2007).
Genome-wide identification and characterization of putative cytochrome P450 genes in the model legume Medicago truncatula.
  Planta, 226, 109-123.  
17606921 M.Makino, H.Sugimoto, Y.Shiro, S.Asamizu, H.Onaka, and S.Nagano (2007).
Crystal structures and catalytic mechanism of cytochrome P450 StaP that produces the indolocarbazole skeleton.
  Proc Natl Acad Sci U S A, 104, 11591-11596.
PDB codes: 2z3t 2z3u
16395678 A.D.Favia, A.Cavalli, M.Masetti, A.Carotti, and M.Recanatini (2006).
Three-dimensional model of the human aromatase enzyme and density functional parameterization of the iron-containing protoporphyrin IX for a molecular dynamics study of heme-cysteinato cytochromes.
  Proteins, 62, 1074-1087.
PDB code: 1tqa
16863466 D.C.Lamb, F.P.Guengerich, S.L.Kelly, and M.R.Waterman (2006).
Exploiting Streptomyces coelicolor A3(2) P450s as a model for application in drug discovery.
  Expert Opin Drug Metab Toxicol, 2, 27-40.  
16825192 D.H.Sherman, S.Li, L.V.Yermalitskaya, Y.Kim, J.A.Smith, M.R.Waterman, and L.M.Podust (2006).
The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae.
  J Biol Chem, 281, 26289-26297.
PDB codes: 2bvj 2c6h 2c7x 2cd8
16637647 K.P.Ravindranathan, E.Gallicchio, R.A.Friesner, A.E.McDermott, and R.M.Levy (2006).
Conformational equilibrium of cytochrome P450 BM-3 complexed with N-palmitoylglycine: a replica exchange molecular dynamics study.
  J Am Chem Soc, 128, 5786-5791.  
15659395 B.Zhao, F.P.Guengerich, A.Bellamine, D.C.Lamb, M.Izumikawa, L.Lei, L.M.Podust, M.Sundaramoorthy, J.A.Kalaitzis, L.M.Reddy, S.L.Kelly, B.S.Moore, D.Stec, M.Voehler, J.R.Falck, T.Shimada, and M.R.Waterman (2005).
Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2.
  J Biol Chem, 280, 11599-11607.
PDB codes: 1s1f 1se6 1t93
16239228 B.Zhao, F.P.Guengerich, M.Voehler, and M.R.Waterman (2005).
Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer.
  J Biol Chem, 280, 42188-42197.
PDB codes: 2d09 2d0e
15834000 D.R.Davydov, A.E.Botchkareva, N.E.Davydova, and J.R.Halpert (2005).
Resolution of two substrate-binding sites in an engineered cytochrome P450eryF bearing a fluorescent probe.
  Biophys J, 89, 418-432.  
15770070 H.Yasui, S.Hayashi, and H.Sakurai (2005).
Possible involvement of singlet oxygen species as multiple oxidants in p450 catalytic reactions.
  Drug Metab Pharmacokinet, 20, 1.  
15617063 J.Mestres (2005).
Structure conservation in cytochromes P450.
  Proteins, 58, 596-609.  
16162505 L.A.McLaughlin, M.J.Paine, C.A.Kemp, J.D.Maréchal, J.U.Flanagan, C.J.Ward, M.J.Sutcliffe, G.C.Roberts, and C.R.Wolf (2005).
Why is quinidine an inhibitor of cytochrome P450 2D6? The role of key active-site residues in quinidine binding.
  J Biol Chem, 280, 38617-38624.  
16269732 V.Jungmann, I.Molnár, P.E.Hammer, D.S.Hill, R.Zirkle, T.G.Buckel, D.Buckel, J.M.Ligon, and J.P.Pachlatko (2005).
Biocatalytic conversion of avermectin to 4"-oxo-avermectin: characterization of biocatalytically active bacterial strains and of cytochrome p450 monooxygenase enzymes and their genes.
  Appl Environ Microbiol, 71, 6968-6976.  
14691240 L.M.Podust, H.Bach, Y.Kim, D.C.Lamb, M.Arase, D.H.Sherman, S.L.Kelly, and M.R.Waterman (2004).
Comparison of the 1.85 A structure of CYP154A1 from Streptomyces coelicolor A3(2) with the closely related CYP154C1 and CYPs from antibiotic biosynthetic pathways.
  Protein Sci, 13, 255-268.
PDB code: 1odo
15189165 O.Pylypenko, and I.Schlichting (2004).
Structural aspects of ligand binding to and electron transfer in bacterial and fungal P450s.
  Annu Rev Biochem, 73, 991.  
15256616 P.A.Williams, J.Cosme, D.M.Vinkovic, A.Ward, H.C.Angove, P.J.Day, C.Vonrhein, I.J.Tickle, and H.Jhoti (2004).
Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone.
  Science, 305, 683-686.
PDB codes: 1w0e 1w0f 1w0g
15256703 T.Tanaka, T.Okuda, and Y.Yamamoto (2004).
Characterization of the CYP3A4 active site by homology modeling.
  Chem Pharm Bull (Tokyo), 52, 830-835.  
12831319 D.F.Lewis (2003).
P450 structures and oxidative metabolism of xenobiotics.
  Pharmacogenomics, 4, 387-395.  
12519760 D.S.Lee, A.Yamada, H.Sugimoto, I.Matsunaga, H.Ogura, K.Ichihara, S.Adachi, S.Y.Park, and Y.Shiro (2003).
Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies.
  J Biol Chem, 278, 9761-9767.
PDB code: 1izo
12514126 G.Sciara, S.G.Kendrew, A.E.Miele, N.G.Marsh, L.Federici, F.Malatesta, G.Schimperna, C.Savino, and B.Vallone (2003).
The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis.
  EMBO J, 22, 205-215.
PDB codes: 1lq9 1n5q 1n5s 1n5t 1n5v
12519772 L.M.Podust, Y.Kim, M.Arase, B.A.Neely, B.J.Beck, H.Bach, D.H.Sherman, D.C.Lamb, S.L.Kelly, and M.R.Waterman (2003).
The 1.92-A structure of Streptomyces coelicolor A3(2) CYP154C1. A new monooxygenase that functionalizes macrolide ring systems.
  J Biol Chem, 278, 12214-12221.
PDB code: 1gwi
14503006 M.A.Schuler, and D.Werck-Reichhart (2003).
Functional genomics of P450s.
  Annu Rev Plant Biol, 54, 629-667.  
12933799 S.Nagano, H.Li, H.Shimizu, C.Nishida, H.Ogura, P.R.Ortiz de Montellano, and T.L.Poulos (2003).
Crystal structures of epothilone D-bound, epothilone B-bound, and substrate-free forms of cytochrome P450epoK.
  J Biol Chem, 278, 44886-44893.
PDB codes: 1pkf 1q5d 1q5e
11943767 D.C.Lamb, T.Skaug, H.L.Song, C.J.Jackson, L.M.Podust, M.R.Waterman, D.B.Kell, D.E.Kelly, and S.L.Kelly (2002).
The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2).
  J Biol Chem, 277, 24000-24005.  
11889110 F.G.Healy, S.B.Krasnoff, M.Wach, D.M.Gibson, and R.Loria (2002).
Involvement of a cytochrome P450 monooxygenase in thaxtomin A biosynthesis by Streptomyces acidiscabies.
  J Bacteriol, 184, 2019-2029.  
12207020 K.Zerbe, O.Pylypenko, F.Vitali, W.Zhang, S.Rouset, M.Heck, J.W.Vrijbloed, D.Bischoff, B.Bister, R.D.Süssmuth, S.Pelzer, W.Wohlleben, J.A.Robinson, and I.Schlichting (2002).
Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis.
  J Biol Chem, 277, 47476-47485.
PDB codes: 1lfk 1lg9 1lgf
12105197 L.Zhang, T.Kudo, N.Takaya, and H.Shoun (2002).
The B' helix determines cytochrome P450nor specificity for the electron donors NADH and NADPH.
  J Biol Chem, 277, 33842-33847.  
11874453 P.Auvray, C.Nativelle, R.Bureau, P.Dallemagne, G.E.Séralini, and P.Sourdaine (2002).
Study of substrate specificity of human aromatase by site directed mutagenesis.
  Eur J Biochem, 269, 1393-1405.  
11959989 P.J.Winn, S.K.Lüdemann, R.Gauges, V.Lounnas, and R.C.Wade (2002).
Comparison of the dynamics of substrate access channels in three cytochrome P450s reveals different opening mechanisms and a novel functional role for a buried arginine.
  Proc Natl Acad Sci U S A, 99, 5361-5366.  
12211002 S.B.Kirton, C.A.Kemp, N.P.Tomkinson, S.St-Gallay, and M.J.Sutcliffe (2002).
Impact of incorporating the 2C5 crystal structure into comparative models of cytochrome P450 2D6.
  Proteins, 49, 216-231.  
12482514 V.Urlacher, and R.D.Schmid (2002).
Biotransformations using prokaryotic P450 monooxygenases.
  Curr Opin Biotechnol, 13, 557-564.  
12207646 Y.Sawada, K.Kinoshita, T.Akashi, T.Aoki, and S.Ayabe (2002).
Key amino acid residues required for aryl migration catalysed by the cytochrome P450 2-hydroxyisoflavanone synthase.
  Plant J, 31, 555-564.  
11606730 A.R.Dunn, I.J.Dmochowski, A.M.Bilwes, H.B.Gray, and B.R.Crane (2001).
Probing the open state of cytochrome P450cam with ruthenium-linker substrates.
  Proc Natl Acad Sci U S A, 98, 12420-12425.
PDB code: 1k2o
11388449 C.Kim, H.Kim, and O.Han (2001).
The role of serine-246 in cytochrome P450eryF-catalyzed hydroxylation of 6-deoxyerythronolide B.
  Biosci Biotechnol Biochem, 65, 752-757.  
11258878 D.S.Lee, S.Y.Park, K.Yamane, E.Obayashi, H.Hori, and Y.Shiro (2001).
Structural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam.
  Biochemistry, 40, 2669-2677.
PDB codes: 1gei 1gej 1gek 1gem
11692080 D.Tsuzuki, C.Takemi, S.Yamamoto, K.Tamagake, S.Imaoka, Y.Funae, H.Kataoka, S.Shinoda, and S.Narimatsu (2001).
Functional evaluation of cytochrome P450 2D6 with Gly42Arg substitution expressed in Saccharomyces cerevisiae.
  Pharmacogenetics, 11, 709-718.  
11248033 L.M.Podust, T.L.Poulos, and M.R.Waterman (2001).
Crystal structure of cytochrome P450 14alpha -sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors.
  Proc Natl Acad Sci U S A, 98, 3068-3073.
PDB codes: 1e9x 1ea1
11737215 N.Sawada, T.Sakaki, S.Kitanaka, S.Kato, and K.Inouye (2001).
Structure-function analysis of CYP27B1 and CYP27A1. Studies on mutants from patients with vitamin D-dependent rickets type I (VDDR-I) and cerebrotendinous xanthomatosis (CTX).
  Eur J Biochem, 268, 6607-6615.  
11150615 C.S.Miles, T.W.Ost, M.A.Noble, A.W.Munro, and S.K.Chapman (2000).
Protein engineering of cytochromes P-450.
  Biochim Biophys Acta, 1543, 383-407.  
11106776 D.F.Lewis, and P.Hlavica (2000).
Interactions between redox partners in various cytochrome P450 systems: functional and structural aspects.
  Biochim Biophys Acta, 1460, 353-374.  
10671516 H.Shimizu, E.Obayashi, Y.Gomi, H.Arakawa, S.Y.Park, H.Nakamura, S.Adachi, H.Shoun, and Y.Shiro (2000).
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.
  J Biol Chem, 275, 4816-4826.
PDB codes: 1cl6 1cmj 1cmn
10662695 I.Molnár, T.Schupp, M.Ono, R.Zirkle, M.Milnamow, B.Nowak-Thompson, N.Engel, C.Toupet, A.Stratmann, D.D.Cyr, J.Gorlach, J.M.Mayo, A.Hu, S.Goff, J.Schmid, and J.M.Ligon (2000).
The biosynthetic gene cluster for the microtubule-stabilizing agents epothilones A and B from Sorangium cellulosum So ce90.
  Chem Biol, 7, 97.  
10716705 J.Cupp-Vickery, R.Anderson, and Z.Hatziris (2000).
Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity.
  Proc Natl Acad Sci U S A, 97, 3050-3055.
PDB codes: 1egy 1eh0 1eup
11094342 J.F.Aparicio, R.Fouces, M.V.Mendes, N.Olivera, and J.F.Martín (2000).
A complex multienzyme system encoded by five polyketide synthase genes is involved in the biosynthesis of the 26-membered polyene macrolide pimaricin in Streptomyces natalensis.
  Chem Biol, 7, 895-905.  
11050228 M.Schalk, and R.Croteau (2000).
A single amino acid substitution (F363I) converts the regiochemistry of the spearmint (-)-limonene hydroxylase from a C6- to a C3-hydroxylase.
  Proc Natl Acad Sci U S A, 97, 11948-11953.  
10704198 Y.T.Chang, and G.Loew (2000).
Homology modeling, molecular dynamics simulations, and analysis of CYP119, a P450 enzyme from extreme acidothermophilic archaeon Sulfolobus solfataricus.
  Biochemistry, 39, 2484-2498.  
10051560 I.F.Sevrioukova, H.Li, H.Zhang, J.A.Peterson, and T.L.Poulos (1999).
Structure of a cytochrome P450-redox partner electron-transfer complex.
  Proc Natl Acad Sci U S A, 96, 1863-1868.
PDB codes: 1bu7 1bvy
10052117 M.Hara, J.Miyake, Y.Asada, and H.Ohkawa (1999).
Purified fusion enzyme between rat cytochrome P4501A1 and yeast NADPH-cytochrome P450 oxidoreductase.
  Biosci Biotechnol Biochem, 63, 21-28.  
9914647 S.Narimatsu, R.Kato, T.Horie, S.Ono, M.Tsutsui, Y.Yabusaki, S.Ohmori, M.Kitada, T.Ichioka, N.Shimada, R.Kato, and T.Ishikawa (1999).
Enantioselectivity of bunitrolol 4-hydroxylation is reversed by the change of an amino acid residue from valine to methionine at position 374 of cytochrome P450-2D6.
  Chirality, 11, 1-9.  
10584064 V.A.Payne, Y.T.Chang, and G.H.Loew (1999).
Homology modeling and substrate binding study of human CYP2C9 enzyme.
  Proteins, 37, 176-190.  
10584066 V.A.Payne, Y.T.Chang, and G.H.Loew (1999).
Homology modeling and substrate binding study of human CYP2C18 and CYP2C19 enzymes.
  Proteins, 37, 204-217.  
10024026 Y.T.Chang, and G.H.Loew (1999).
Homology modeling and substrate binding study of human CYP4A11 enzyme.
  Proteins, 34, 403-415.  
9520404 A.D.Vaz, D.F.McGinnity, and M.J.Coon (1998).
Epoxidation of olefins by cytochrome P450: evidence from site-specific mutagenesis for hydroperoxo-iron as an electrophilic oxidant.
  Proc Natl Acad Sci U S A, 95, 3555-3560.  
9497336 A.Nikoshkov, S.Lajic, A.Vlamis-Gardikas, L.Tranebjaerg, M.Holst, A.Wedell, and H.Luthman (1998).
Naturally occurring mutants of human steroid 21-hydroxylase (P450c21) pinpoint residues important for enzyme activity and stability.
  J Biol Chem, 273, 6163-6165.  
9630657 D.F.Lewis, E.Watson, and B.G.Lake (1998).
Evolution of the cytochrome P450 superfamily: sequence alignments and pharmacogenetics.
  Mutat Res, 410, 245-270.  
9851289 D.F.Lewis, P.J.Eddershaw, M.Dickins, M.H.Tarbit, and P.S.Goldfarb (1998).
Structural determinants of cytochrome P450 substrate specificity, binding affinity and catalytic rate.
  Chem Biol Interact, 115, 175-199.  
9722531 E.A.Dierks, Z.Zhang, E.F.Johnson, and P.R.de Montellano (1998).
The catalytic site of cytochrome P4504A11 (CYP4A11) and its L131F mutant.
  J Biol Chem, 273, 23055-23061.  
9442050 I.Sagami, and T.Shimizu (1998).
The crucial roles of Asp-314 and Thr-315 in the catalytic activation of molecular oxygen by neuronal nitric-oxide synthase. A site-directed mutagenesis study.
  J Biol Chem, 273, 2105-2108.  
9753700 J.A.Peterson, and S.E.Graham (1998).
A close family resemblance: the importance of structure in understanding cytochromes P450.
  Structure, 6, 1079-1085.  
9837822 J.T.Wang, C.J.Lin, S.M.Burridge, G.K.Fu, M.Labuda, A.A.Portale, and W.L.Miller (1998).
Genetics of vitamin D 1alpha-hydroxylase deficiency in 17 families.
  Am J Hum Genet, 63, 1694-1702.  
9649301 M.Vidakovic, S.G.Sligar, H.Li, and T.L.Poulos (1998).
Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect.
  Biochemistry, 37, 9211-9219.
PDB codes: 5cp4 6cp4
9636024 N.Okamoto, Y.Imai, H.Shoun, and Y.Shiro (1998).
Site-directed mutagenesis of the conserved threonine (Thr243) of the distal helix of fungal cytochrome P450nor.
  Biochemistry, 37, 8839-8847.  
  9435150 Y.C.Kao, C.Zhou, M.Sherman, C.A.Laughton, and S.Chen (1998).
Molecular basis of the inhibition of human aromatase (estrogen synthetase) by flavone and isoflavone phytoestrogens: A site-directed mutagenesis study.
  Environ Health Perspect, 106, 85-92.  
9831532 Y.Xue, D.Wilson, L.Zhao, H.Liu, and D.H.Sherman (1998).
Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae.
  Chem Biol, 5, 661-667.  
9048540 C.F.Oliver, S.Modi, M.J.Sutcliffe, W.U.Primrose, L.Y.Lian, and G.C.Roberts (1997).
A single mutation in cytochrome P450 BM3 changes substrate orientation in a catalytic intermediate and the regiospecificity of hydroxylation.
  Biochemistry, 36, 1567-1572.  
9206006 D.G.Kellner, S.A.Maves, and S.G.Sligar (1997).
Engineering cytochrome P450s for bioremediation.
  Curr Opin Biotechnol, 8, 274-278.  
9428674 F.Bancel, N.Bec, C.Ebel, and R.Lange (1997).
A central role for water in the control of the spin state of cytochrome P-450scc.
  Eur J Biochem, 250, 276-285.  
8995412 S.Graham-Lorence, G.Truan, J.A.Peterson, J.R.Falck, S.Wei, C.Helvig, and J.H.Capdevila (1997).
An active site substitution, F87V, converts cytochrome P450 BM-3 into a regio- and stereoselective (14S,15R)-arachidonic acid epoxygenase.
  J Biol Chem, 272, 1127-1135.  
9122160 T.I.Oprea, G.Hummer, and A.E.Garcia (1997).
Identification of a functional water channel in cytochrome P450 enzymes.
  Proc Natl Acad Sci U S A, 94, 2133-2138.  
8643457 A.D.Vaz, S.J.Pernecky, G.M.Raner, and M.J.Coon (1996).
Peroxo-iron and oxenoid-iron species as alternative oxygenating agents in cytochrome P450-catalyzed reactions: switching by threonine-302 to alanine mutagenesis of cytochrome P450 2B4.
  Proc Natl Acad Sci U S A, 93, 4644-4648.  
8809764 A.W.Munro, and J.G.Lindsay (1996).
Bacterial cytochromes P-450.
  Mol Microbiol, 20, 1115-1125.  
9010604 E.F.Kolesanova, J.G.Kiselar, C.Jung, S.A.Kozin, G.Hui Bon Hoa, and A.I.Archakov (1996).
Antigenic mapping of bacterial and animal cytochromes P-450.
  Biochimie, 78, 752-762.  
8898299 E.H.Oliw, J.Bylund, and C.Herman (1996).
Bisallylic hydroxylation and epoxidation of polyunsaturated fatty acids by cytochrome P450.
  Lipids, 31, 1003-1021.  
9010597 H.Li, and T.L.Poulos (1996).
Conformational dynamics in cytochrome P450-substrate interactions.
  Biochimie, 78, 695-699.  
8798438 J.H.Capdevila, S.Wei, C.Helvig, J.R.Falck, Y.Belosludtsev, G.Truan, S.E.Graham-Lorence, and J.A.Peterson (1996).
The highly stereoselective oxidation of polyunsaturated fatty acids by cytochrome P450BM-3.
  J Biol Chem, 271, 22663-22671.  
8621484 R.Nakano, H.Sato, A.Watanabe, O.Ito, and T.Shimizu (1996).
Conserved Glu318 at the cytochrome P450 1A2 distal site is crucial in the nitric oxide complex stability.
  J Biol Chem, 271, 8570-8574.  
9010609 T.Kudo, D.Tomura, D.L.Liu, X.Q.Dai, and H.Shoun (1996).
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.
  Biochimie, 78, 792-799.  
8747463 M.Sundaramoorthy, J.Terner, and T.L.Poulos (1995).
The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid.
  Structure, 3, 1367-1377.
PDB codes: 1cpo 2cpo
8749843 R.W.Harrison, D.Chatterjee, and I.T.Weber (1995).
Analysis of six protein structures predicted by comparative modeling techniques.
  Proteins, 23, 463-471.  
8749364 T.L.Poulos (1995).
Cytochrome P450.
  Curr Opin Struct Biol, 5, 767-774.  
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 codes are shown on the right.