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PDBsum entry 1cpp

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Oxidoreductase(oxygenase) PDB id
1cpp
Contents
Protein chain
405 a.a.*
Ligands
HEM
CAM
* C-alpha coords only
Superseded by: 2cpp
PDB id:
1cpp
Name: Oxidoreductase(oxygenase)
Structure: Cytochrome p450 ( CAM )
Source: (Pseudomonas putida)
Authors: T.L.Poulos,B.C.Finzel,I.R.Gunsalus,G.C.Wagner,J.Kraut
Key ref: T.L.Poulos et al. (1985). The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450. J Biol Chem, 260, 16122-16130. PubMed id: 4066706
Date:
21-Nov-85     Release date:   21-Jan-86    
 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 405 a.a.
Key:    Secondary structure

 

 
    Key reference    
 
 
J Biol Chem 260:16122-16130 (1985)
PubMed id: 4066706  
 
 
The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450.
T.L.Poulos, B.C.Finzel, I.C.Gunsalus, G.C.Wagner, J.Kraut.
 
  ABSTRACT  
 
The crystal structure of Pseudomonas putida cytochrome P-450cam in the ferric, camphor bound form has been determined and partially refined to R = 0.23 at 2.6 A. The single 414 amino acid polypeptide chain (Mr = 45,000) approximates a triangular prism with a maximum dimension of approximately 60 A and a minimum of approximately 30 A. Twelve helical segments (A through L) account for approximately 40% of the structure while antiparallel beta pairs account for only approximately 10%. The unexposed iron protoporphyrin IX is sandwiched between two parallel helices designated the proximal and distal helices. The heme iron atom is pentacoordinate with the axial sulfur ligand provided by Cys 357 which extends from the N-terminal end of the proximal (L) helix. A substrate molecule, 2-bornanone (camphor), is buried in an internal pocket just above the heme distal surface adjacent to the oxygen binding site. The substrate molecule is held in place by a hydrogen bond between the side chain hydroxyl group of Tyr 96 and the camphor carbonyl oxygen atom in addition to complementary hydrophobic contacts between the camphor molecule and neighboring aliphatic and aromatic residues. The camphor is oriented such that the exo-surface of C5 would contact an iron bound, "activated" oxygen atom for stereoselective hydroxylation.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20428921 K.Toda, R.Takahashi, T.Iwashina, and M.Hajika (2011).
Difference in chilling-induced flavonoid profiles, antioxidant activity and chilling tolerance between soybean near-isogenic lines for the pubescence color gene.
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The extreme dwarf phenotype of the GA-sensitive mutant of sunflower, dwarf2, is generated by a deletion in the ent-kaurenoic acid oxidase1 (HaKAO1) gene sequence.
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21171581 Y.T.Lee, E.C.Glazer, R.F.Wilson, C.D.Stout, and D.B.Goodin (2011).
Three clusters of conformational States in p450cam reveal a multistep pathway for closing of the substrate access channel .
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20361237 A.Tarcsay, R.Kiss, and G.M.Keseru (2010).
Site of metabolism prediction on cytochrome P450 2C9: a knowledge-based docking approach.
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20297780 Y.T.Lee, R.F.Wilson, I.Rupniewski, and D.B.Goodin (2010).
P450cam visits an open conformation in the absence of substrate.
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PDB codes: 3l61 3l62 3l63
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The 1.5-A structure of XplA-heme, an unusual cytochrome P450 heme domain that catalyzes reductive biotransformation of royal demolition explosive.
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PDB codes: 2wiv 2wiy
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18622598 E.M.Isin, and F.P.Guengerich (2008).
Substrate binding to cytochromes P450.
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18976212 K.N.Myasoedova (2008).
New findings in studies of cytochromes P450.
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Combined QM/MM calculations of active-site vibrations in binding process of P450cam to putidaredoxin.
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Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.
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PDB codes: 3ejb 3ejd 3eje
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Structural evidence for a functionally relevant second camphor binding site in P450cam: model for substrate entry into a P450 active site.
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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.
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CO migration pathways in cytochrome P450cam studied by molecular dynamics simulations.
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Crystallographic evidence for dioxygen interactions with iron proteins.
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PDB codes: 2z3t 2z3u
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Putidaredoxin-to-cytochrome P450cam electron transfer: differences between the two reductive steps required for catalysis.
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Cryoreduction EPR and 13C, 19F ENDOR study of substrate-bound substates and solvent kinetic isotope effects in the catalytic cycle of cytochrome P450cam and its T252A mutant.
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15189165 O.Pylypenko, and I.Schlichting (2004).
Structural aspects of ligand binding to and electron transfer in bacterial and fungal P450s.
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Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks.
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Key amino acid residues required for aryl migration catalysed by the cytochrome P450 2-hydroxyisoflavanone synthase.
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Probing the open state of cytochrome P450cam with ruthenium-linker substrates.
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PDB code: 1k2o
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  Proc Natl Acad Sci U S A, 98, 3068-3073.
PDB codes: 1e9x 1ea1
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Fine-mapping, mutation analyses, and structural mapping of cerebrotendinous xanthomatosis in U.S. pedigrees.
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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.  
10681464 A.K.Hull, R.Vij, and J.L.Celenza (2000).
Arabidopsis cytochrome P450s that catalyze the first step of tryptophan-dependent indole-3-acetic acid biosynthesis.
  Proc Natl Acad Sci U S A, 97, 2379-2384.  
11087371 C.Tetreau, M.Tourbez, and D.Lavalette (2000).
Conformational relaxation in hemoproteins: the cytochrome P-450cam case.
  Biochemistry, 39, 14219-14231.  
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Sequencing and analysis of the Mmethylococcus capsulatus (Bath) solublemethane monooxygenase genes.
  Eur J Biochem, 267, 2174-2185.  
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Cytochromes P450: a success story.
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10678174 P.A.Williams, J.Cosme, V.Sridhar, E.F.Johnson, and D.E.McRee (2000).
Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity.
  Mol Cell, 5, 121-131.
PDB code: 1dt6
16232916 T.Sakaki, and K.Inouye (2000).
Practical application of mammalian cytochrome P450.
  J Biosci Bioeng, 90, 583-590.  
10998236 Y.Furukawa, K.Ishimori, and I.Morishima (2000).
Electron transfer reactions in Zn-substituted cytochrome P450cam.
  Biochemistry, 39, 10996-11004.  
10220313 A.Parikh, P.D.Josephy, and F.P.Guengerich (1999).
Selection and characterization of human cytochrome P450 1A2 mutants with altered catalytic properties.
  Biochemistry, 38, 5283-5289.  
10353832 C.Tetreau, M.Tourbez, A.Gorren, B.Mayer, and D.Lavalette (1999).
Dynamics of carbon monoxide binding with neuronal nitric oxide synthase.
  Biochemistry, 38, 7210-7218.  
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
10320335 M.Schalk, S.Nedelkina, G.Schoch, Y.Batard, and D.Werck-Reichhart (1999).
Role of unusual amino acid residues in the proximal and distal heme regions of a plant P450, CYP73A1.
  Biochemistry, 38, 6093-6103.  
10194363 S.K.Lee, and J.D.Lipscomb (1999).
Oxygen activation catalyzed by methane monooxygenase hydroxylase component: proton delivery during the O-O bond cleavage steps.
  Biochemistry, 38, 4423-4432.  
9761931 D.Nickerson, L.L.Wong, and Z.Rao (1998).
An improved procedure for the preparation of X-ray diffraction-quality crystals of cytochrome p450cam.
  Acta Crystallogr D Biol Crystallogr, 54, 470-472.  
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.  
9636025 M.Shimoji, H.Yin, L.Higgins, and J.P.Jones (1998).
Design of a novel P450: a functional bacterial-human cytochrome P450 chimera.
  Biochemistry, 37, 8848-8852.  
  9484813 N.Harada, and O.Hatano (1998).
Inhibitors of aromatase prevent degradation of the enzyme in cultured human tumour cells.
  Br J Cancer, 77, 567-572.  
  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.  
9109669 J.Wang, D.J.Stuehr, and D.L.Rousseau (1997).
Interactions between substrate analogues and heme ligands in nitric oxide synthase.
  Biochemistry, 36, 4595-4606.  
  9293186 L.Thöny-Meyer (1997).
Biogenesis of respiratory cytochromes in bacteria.
  Microbiol Mol Biol Rev, 61, 337-376.  
9256362 M.H.Bassett, J.L.McCarthy, M.R.Waterman, and T.J.Sliter (1997).
Sequence and developmental expression of Cyp18, a member of a new cytochrome P450 family from Drosophila.
  Mol Cell Endocrinol, 131, 39-49.  
9223185 P.Jean, J.Pothier, P.M.Dansette, D.Mansuy, and A.Viari (1997).
Automated multiple analysis of protein structures: application to homology modeling of cytochromes P450.
  Proteins, 28, 388-404.  
9311133 Y.Yang, D.Zhang, and C.E.Cerniglia (1997).
Purification and characterization of a cytosolic cytochrome P450 from yeast Trichosporon cutaneum.
  FEMS Microbiol Lett, 154, 347-353.  
8611587 C.Galli, R.MacArthur, H.M.Abu-Soud, P.Clark, D.J.Steuhr, and G.W.Brudvig (1996).
EPR spectroscopic characterization of neuronal NO synthase.
  Biochemistry, 35, 2804-2810.  
8634274 D.K.Ghosh, H.M.Abu-Soud, and D.J.Stuehr (1996).
Domains of macrophage N(O) synthase have divergent roles in forming and stabilizing the active dimeric enzyme.
  Biochemistry, 35, 1444-1449.  
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.  
9010605 K.Wakasugi, K.Ishimori, and I.Morishima (1996).
NMR studies of recombinant cytochrome P450cam mutants.
  Biochimie, 78, 763-770.  
8755738 R.M.Chabin, E.McCauley, J.R.Calaycay, T.M.Kelly, K.L.MacNaul, G.C.Wolfe, N.I.Hutchinson, S.Madhusudanaraju, J.A.Schmidt, J.W.Kozarich, and K.K.Wong (1996).
Active-site structure analysis of recombinant human inducible nitric oxide synthase using imidazole.
  Biochemistry, 35, 9567-9575.  
8931549 S.A.Martinis, S.R.Blanke, L.P.Hager, S.G.Sligar, G.H.Hoa, J.J.Rux, and J.H.Dawson (1996).
Probing the heme iron coordination structure of pressure-induced cytochrome P420cam.
  Biochemistry, 35, 14530-14536.  
8874031 S.Kumar, and M.Bansal (1996).
Structural and sequence characteristics of long alpha helices in globular proteins.
  Biophys J, 71, 1574-1586.  
8855949 T.Matsui, S.Nagano, K.Ishimori, Y.Watanabe, and I.Morishima (1996).
Preparation and reactions of myoglobin mutants bearing both proximal cysteine ligand and hydrophobic distal cavity: protein models for the active site of P-450.
  Biochemistry, 35, 13118-13124.  
9010607 Uvarov VYu, Y.D.Ivanov, A.N.Romanov, M.O.Gallyamov, O.I.Kiselyova, and I.V.Yaminsky (1996).
Scanning tunneling microscopy study of cytochrome P450 2B4 incorporated in proteoliposomes.
  Biochimie, 78, 780-784.  
  8843297 Y.Mizuki, I.Fujiwara, T.Yamaguchi, and Y.Sekine (1996).
Structure-related inhibitory effect of antimicrobial enoxacin and derivatives on theophylline metabolism by rat liver microsomes.
  Antimicrob Agents Chemother, 40, 1875-1880.  
7743131 C.A.Hasemann, R.G.Kurumbail, S.S.Boddupalli, J.A.Peterson, and J.Deisenhofer (1995).
Structure and function of cytochromes P450: a comparative analysis of three crystal structures.
  Structure, 3, 41-62.  
7612848 C.Di Primo, E.Deprez, G.H.Hoa, and P.Douzou (1995).
Antagonistic effects of hydrostatic pressure and osmotic pressure on cytochrome P-450cam spin transition.
  Biophys J, 68, 2056-2061.  
  7645302 D.F.Lewis (1995).
Three-dimensional models of human and other mammalian microsomal P450s constructed from an alignment with P450102 (P450bm3).
  Xenobiotica, 25, 333-366.  
7819285 M.Kato, R.Makino, and T.Iizuka (1995).
Thermodynamic aspects of the CO-binding reaction to cytochrome P-450cam. Relevance with their biological significance and structure.
  Biochim Biophys Acta, 1246, 178-184.  
7492620 M.Tsubaki, K.Morimoto, S.Tomita, S.Miura, Y.Ichikawa, A.Miyatake, F.Masuya, and H.Hori (1995).
Electron paramagnetic resonance investigation of cytochrome P-450c21 from bovine adrenocortical microsomes: a new enzymatic activity.
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7892226 P.F.Kraus, and T.M.Kutchan (1995).
Molecular cloning and heterologous expression of a cDNA encoding berbamunine synthase, a C--O phenol-coupling cytochrome P450 from the higher plant Berberis stolonifera.
  Proc Natl Acad Sci U S A, 92, 2071-2075.  
8076220 O.P.Mgbonyebi, C.T.Smothers, and J.J.Mrotek (1994).
Modulation of adrenal cell functions by cadmium salts: 2. Sites affected by CdCl2 during unstimulated steroid synthesis.
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  7989540 P.Burgener-Kairuz, J.P.Zuber, P.Jaunin, T.G.Buchman, J.Bille, and M.Rossier (1994).
Rapid detection and identification of Candida albicans and Torulopsis (Candida) glabrata in clinical specimens by species-specific nested PCR amplification of a cytochrome P-450 lanosterol-alpha-demethylase (L1A1) gene fragment.
  J Clin Microbiol, 32, 1902-1907.  
7813487 R.Lange, P.Anzenbacher, S.Müller, L.Maurin, and C.Balny (1994).
Interaction of tryptophan residues of cytochrome P450scc with a highly specific fluorescence quencher, a substrate analogue, compared to acrylamide and iodide.
  Eur J Biochem, 226, 963-970.  
  8387235 D.F.Lewis, and B.G.Lake (1993).
Interaction of some peroxisome proliferators with the mouse liver peroxisome proliferator-activated receptor (PPAR): a molecular modelling and quantitative structure-activity relationship (QSAR) study.
  Xenobiotica, 23, 79-96.  
7678494 D.R.Nelson, T.Kamataki, D.J.Waxman, F.P.Guengerich, R.W.Estabrook, R.Feyereisen, F.J.Gonzalez, M.J.Coon, I.C.Gunsalus, and O.Gotoh (1993).
The P450 superfamily: update on new sequences, gene mapping, accession numbers, early trivial names of enzymes, and nomenclature.
  DNA Cell Biol, 12, 1.  
  8416893 D.Stassi, S.Donadio, M.J.Staver, and L.Katz (1993).
Identification of a Saccharopolyspora erythraea gene required for the final hydroxylation step in erythromycin biosynthesis.
  J Bacteriol, 175, 182-189.  
8121931 K.Ruckpaul (1993).
[Cytochrome p-450 dependent enzymes--target enzymes for drug action?]
  Pharm Unserer Zeit, 22, 296-304.  
8377025 L.M.Koymans, N.P.Vermeulen, A.Baarslag, and G.M.Donné-Op den Kelder (1993).
A preliminary 3D model for cytochrome P450 2D6 constructed by homology model building.
  J Comput Aided Mol Des, 7, 281-289.  
7763853 M.S.Logan, L.M.Newman, C.A.Schanke, and L.P.Wackett (1993).
Cosubstrate effects in reductive dehalogenation by Pseudomonas putida G786 expressing cytochrome P-450CAM.
  Biodegradation, 4, 39-50.  
7683828 R.C.Prince, and D.E.Gunson (1993).
Rising interest in nitric oxide synthase.
  Trends Biochem Sci, 18, 35-36.  
8464872 S.J.Pernecky, J.R.Larson, R.M.Philpot, and M.J.Coon (1993).
Expression of truncated forms of liver microsomal P450 cytochromes 2B4 and 2E1 in Escherichia coli: influence of NH2-terminal region on localization in cytosol and membranes.
  Proc Natl Acad Sci U S A, 90, 2651-2655.  
1425665 C.Di Primo, G.Hui Bon Hoa, P.Douzou, and S.G.Sligar (1992).
Heme-pocket-hydration change during the inactivation of cytochrome P-450camphor by hydrostatic pressure.
  Eur J Biochem, 209, 583-588.  
1517776 D.F.Lewis, and H.Moereels (1992).
The sequence homologies of cytochromes P-450 and active-site geometries.
  J Comput Aided Mol Des, 6, 235-252.  
  1455898 M.J.Humphrey, and D.A.Smith (1992).
Role of metabolism and pharmacokinetic studies in the discovery of new drugs--present and future perspectives.
  Xenobiotica, 22, 743-755.  
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Observation of the FeIV=O stretching Raman band for a thiolate-ligated heme protein. Compound I of chloroperoxidase.
  FEBS Lett, 305, 206-208.  
1656462 J.R.Larson, M.J.Coon, and T.D.Porter (1991).
Purification and properties of a shortened form of cytochrome P-450 2E1: deletion of the NH2-terminal membrane-insertion signal peptide does not alter the catalytic activities.
  Proc Natl Acad Sci U S A, 88, 9141-9145.  
1652267 P.M.Kroneck, W.Jakob, D.A.Webster, and R.DeMaio (1991).
Studies on the bacterial hemoglobin from Vitreoscilla. Redox properties and spectroscopic characterization of the different forms of the hemoprotein.
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The involvement of free radicals in the mechanisms of monooxygenases.
  Pharmacol Ther, 49, 21-42.  
  2345149 C.A.Omer, R.Lenstra, P.J.Litle, C.Dean, J.M.Tepperman, K.J.Leto, J.A.Romesser, and D.P.O'Keefe (1990).
Genes for two herbicide-inducible cytochromes P-450 from Streptomyces griseolus.
  J Bacteriol, 172, 3335-3345.  
2226459 C.Di Primo, G.Hui Bon Hoa, P.Douzou, and S.Sligar (1990).
Effect of the tyrosine 96 hydrogen bond on the inactivation of cytochrome P-450cam induced by hydrostatic pressure.
  Eur J Biochem, 193, 383-386.  
2326187 C.Hassett, and C.J.Omiecinski (1990).
Sequence and gene expression of rabbit cytochrome P450 IIC16: comparison to highly related family members.
  Nucleic Acids Res, 18, 1429-1434.  
2405436 D.E.Ryan, and W.Levin (1990).
Purification and characterization of hepatic microsomal cytochrome P-450.
  Pharmacol Ther, 45, 153-239.  
2213061 H.Moereels, L.De Bie, and J.P.Tollenaere (1990).
CGEMA and VGAP: a Colour Graphics Editor for Multiple Alignment using a variable GAP penalty. Application to the muscarinic acetylcholine receptor.
  J Comput Aided Mol Des, 4, 131-145.  
1692626 K.R.Bozak, H.Yu, R.Sirevåg, and R.E.Christoffersen (1990).
Sequence analysis of ripening-related cytochrome P-450 cDNAs from avocado fruit.
  Proc Natl Acad Sci U S A, 87, 3904-3908.  
2176109 K.Shikama (1990).
Autoxidation of oxymyoglobin: a meeting point of the stabilization and the activation of molecular oxygen.
  Biol Rev Camb Philos Soc, 65, 517-527.  
  2123860 P.J.Lammers, S.McLaughlin, S.Papin, C.Trujillo-Provencio, and A.J.Ryncarz (1990).
Developmental rearrangement of cyanobacterial nif genes: nucleotide sequence, open reading frames, and cytochrome P-450 homology of the Anabaena sp. strain PCC 7120 nifD element.
  J Bacteriol, 172, 6981-6990.  
2213064 R.C.Wade (1990).
Solvation of the active site of cytochrome P450-cam.
  J Comput Aided Mol Des, 4, 199-204.  
2328295 T.Sasaki, and E.T.Kaiser (1990).
Synthesis and structural stability of helichrome as an artificial hemeproteins.
  Biopolymers, 29, 79-88.  
2676531 D.Mansuy, P.Battioni, and J.P.Battioni (1989).
Chemical model systems for drug-metabolizing cytochrome-P-450-dependent monooxygenases.
  Eur J Biochem, 184, 267-285.  
2750591 E.Rekka, H.Timmermann, and A.Bast (1989).
Structural features of some diphenhydramine analogues that determine the interaction with rat liver cytochrome P-450.
  Agents Actions, 27, 184-187.  
2510153 M.Imai, H.Shimada, Y.Watanabe, Y.Matsushima-Hibiya, R.Makino, H.Koga, T.Horiuchi, and Y.Ishimura (1989).
Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: possible role of the hydroxy amino acid in oxygen activation.
  Proc Natl Acad Sci U S A, 86, 7823-7827.  
2598933 P.Hildebrandt, R.Greinert, A.Stier, and H.Taniguchi (1989).
Resonance Raman study on the structure of the active sites of microsomal cytochrome P-450 isozymes LM2 and LM4.
  Eur J Biochem, 186, 291-302.  
2922393 R.Feyereisen, J.F.Koener, D.E.Farnsworth, and D.W.Nebert (1989).
Isolation and sequence of cDNA encoding a cytochrome P-450 from an insecticide-resistant strain of the house fly, Musca domestica.
  Proc Natl Acad Sci U S A, 86, 1465-1469.  
  2708311 R.H.Kanemoto, A.T.Powell, D.E.Akiyoshi, D.A.Regier, R.A.Kerstetter, E.W.Nester, M.C.Hawes, and M.P.Gordon (1989).
Nucleotide sequence and analysis of the plant-inducible locus pinF from Agrobacterium tumefaciens.
  J Bacteriol, 171, 2506-2512.  
2509201 T.Matsuoka, S.Miyakoshi, K.Tanzawa, K.Nakahara, M.Hosobuchi, and N.Serizawa (1989).
Purification and characterization of cytochrome P-450sca from Streptomyces carbophilus. ML-236B (compactin) induces a cytochrome P-450sca in Streptomyces carbophilus that hydroxylates ML-236B to pravastatin sodium (CS-514), a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase.
  Eur J Biochem, 184, 707-713.  
2714291 Uvarov VYu, V.E.Tretiakov, A.V.Leshchenko, I.G.Rukavishnikov, C.S.Dzhuzenova, L.Z.Tretiakova, and A.I.Archakov (1989).
Effect of the microenvironment on the tertiary structure of cytochrome P-450 LM2.
  Eur J Biochem, 181, 391-396.  
2848247 C.J.Corbin, S.Graham-Lorence, M.McPhaul, J.I.Mason, C.R.Mendelson, and E.R.Simpson (1988).
Isolation of a full-length cDNA insert encoding human aromatase system cytochrome P-450 and its expression in nonsteroidogenic cells.
  Proc Natl Acad Sci U S A, 85, 8948-8952.  
3278179 J.P.Tollenaere, and P.A.Janssen (1988).
Conformational analysis and computer graphics in drug research.
  Med Res Rev, 8, 1.  
  3390233 S.A.Chen, M.J.Besman, R.S.Sparkes, S.Zollman, I.Klisak, T.Mohandas, P.F.Hall, and J.E.Shively (1988).
Human aromatase: cDNA cloning, Southern blot analysis, and assignment of the gene to chromosome 15.
  DNA, 7, 27-38.  
3050990 V.F.Kalb, and J.C.Loper (1988).
Proteins from eight eukaryotic cytochrome P-450 families share a segmented region of sequence similarity.
  Proc Natl Acad Sci U S A, 85, 7221-7225.  
3322951 H.B.Dunford (1987).
Free radicals in iron-containing systems.
  Free Radic Biol Med, 3, 405-421.  
3322950 I.Yamazaki (1987).
Free radical mechanisms in enzyme reactions.
  Free Radic Biol Med, 3, 397-404.  
  3549208 T.Sakaki, M.Shibata, Y.Yabusaki, and H.Ohkawa (1987).
Expression in Saccharomyces cerevisiae of chimeric cytochrome P450 cDNAs constructed from cDNAs for rat cytochrome P450c and P450d.
  DNA, 6, 31-39.  
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.

 

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