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PDBsum entry 1phc
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Oxidoreductase(oxygenase) PDB id
1phc

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
405 a.a. *
Ligands
HEM
Waters ×192
* Residue conservation analysis
PDB id:
1phc
Name: Oxidoreductase(oxygenase)
Title: Crystal structure of substrate-free pseudomonas putida cytochrome p450
Structure: Cytochrome p450-cam. Chain: a. Engineered: yes
Source: Pseudomonas putida. Organism_taxid: 303
Resolution:
1.60Å     R-factor:   0.190    
Authors: T.L.Poulos
Key ref:
T.L.Poulos et al. (1986). Crystal structure of substrate-free Pseudomonas putida cytochrome P-450. Biochemistry, 25, 5314-5322. PubMed id: 3768350 DOI: 10.1021/bi00366a049
Date:
27-Jul-92     Release date:   31-Oct-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00183  (CPXA_PSEPU) -  Camphor 5-monooxygenase from Pseudomonas putida
Seq:
Struc: 		415 a.a.
405 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.14.15.1  - camphor 5-monooxygenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 reduced [2Fe-2S]-[putidaredoxin] + (1R,4R)-camphor + O2 + 2 H+ = (1R,4R,5R)-5-hydroxycamphor + 2 oxidized [2Fe-2S]-[putidaredoxin] + H2O
2 × reduced [2Fe-2S]-[putidaredoxin]
 + (1R,4R)-camphor
 + O2
 + 2 × H(+)
 = (1R,4R,5R)-5-hydroxycamphor
 + 2 × oxidized [2Fe-2S]-[putidaredoxin]
 + H2O
      Cofactor: Heme-thiolate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Key reference    
 
 
DOI no: 10.1021/bi00366a049 Biochemistry 25:5314-5322 (1986)
PubMed id: 3768350  
 
 
Crystal structure of substrate-free Pseudomonas putida cytochrome P-450.
T.L.Poulos, B.C.Finzel, A.J.Howard.
 
  ABSTRACT  
 
The crystal structure of Pseudomonas putida cytochrome P-450cam in the substrate-free form has been refined at 2.20-A resolution and compared to the substrate-bound form of the enzyme. In the absence of the substrate camphor, the P-450cam heme iron atom is hexacoordinate with the sulfur atom of Cys-357 providing one axial heme ligand and a water molecule or hydroxide ion providing the other axial ligand. A network of hydrogen-bonded solvent molecules occupies the substrate pocket in addition to the iron-linked aqua ligand. When a camphor molecule binds, the active site waters including the aqua ligand are displaced, resulting in a pentacoordinate high-spin heme iron atom. Analysis of the Fno camphor - F camphor difference Fourier and a quantitative comparison of the two refined structures reveal that no detectable conformational change results from camphor binding other than a small repositioning of a phenylalanine side chain that contacts the camphor molecule. However, large decreases in the mean temperature factors of three separate segments of the protein centered on Tyr-96, Thr-185, and Asp-251 result from camphor binding. This indicates that camphor binding decreases the flexibility in these three regions of the P-450cam molecule without altering the mean position of the atoms involved.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21279813 M.Fambrini, L.Mariotti, S.Parlanti, P.Picciarelli, M.Salvini, N.Ceccarelli, and C.Pugliesi (2011).
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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21154803 M.Ma, S.G.Bell, W.Yang, Y.Hao, N.H.Rees, M.Bartlam, W.Zhou, L.L.Wong, and Z.Rao (2011).
Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444.
  Chembiochem, 12, 88-99.
PDB codes: 3oft 3ofu
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).
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20544970 L.J.Smith, A.Kahraman, and J.M.Thornton (2010).
Heme proteins--diversity in structural characteristics, function, and folding.
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20013305 L.Sun, Z.H.Wang, F.Y.Ni, X.S.Tan, and Z.X.Huang (2010).
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21149675 L.V.Liu, C.B.Bell, S.D.Wong, S.A.Wilson, Y.Kwak, M.S.Chow, J.Zhao, K.O.Hodgson, B.Hedman, and E.I.Solomon (2010).
Definition of the intermediates and mechanism of the anticancer drug bleomycin using nuclear resonance vibrational spectroscopy and related methods.
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19947890 N.Shakunthala (2010).
New cytochrome P450 mechanisms: implications for understanding molecular basis for drug toxicity at the level of the cytochrome.
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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.
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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.
  Biochemistry, 49, 3412-3419.
PDB codes: 3l61 3l62 3l63
19438234 A.Dey, Y.Jiang, P.Ortiz de Montellano, K.O.Hodgson, B.Hedman, and E.I.Solomon (2009).
S K-edge XAS and DFT calculations on cytochrome P450: covalent and ionic contributions to the cysteine-Fe bond and their contribution to reactivity.
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19199046 C.R.McCullough, P.K.Pullela, S.C.Im, L.Waskell, and D.S.Sem (2009).
(13)C-Methyl isocyanide as an NMR probe for cytochrome P450 active sites.
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Substrate binding induces structural changes in cytochrome P450cam.
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PDB codes: 2zwt 2zwu
19265398 S.Balaz (2009).
Modeling kinetics of subcellular disposition of chemicals.
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19283807 T.K.Yanai, and S.Mori (2009).
Density functional studies on isomerization of prostaglandin H2 to prostacyclin catalyzed by cytochrome P450.
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18513977 B.OuYang, S.S.Pochapsky, M.Dang, and T.C.Pochapsky (2008).
A functional proline switch in cytochrome P450cam.
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18622598 E.M.Isin, and F.P.Guengerich (2008).
Substrate binding to cytochromes P450.
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18026129 J.D.Maréchal, C.A.Kemp, G.C.Roberts, M.J.Paine, C.R.Wolf, and M.J.Sutcliffe (2008).
Insights into drug metabolism by cytochromes P450 from modelling studies of CYP2D6-drug interactions.
  Br J Pharmacol, 153, S82-S89.  
18976212 K.N.Myasoedova (2008).
New findings in studies of cytochromes P450.
  Biochemistry (Mosc), 73, 965-969.  
18844316 T.K.Yanai, and S.Mori (2008).
Density functional studies on thromboxane biosynthesis: mechanism and role of the heme-thiolate system.
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18023482 Y.Hamuro, K.S.Molnar, S.J.Coales, B.OuYang, A.K.Simorellis, and T.C.Pochapsky (2008).
Hydrogen-deuterium exchange mass spectrometry for investigation of backbone dynamics of oxidized and reduced cytochrome P450cam.
  J Inorg Biochem, 102, 364-370.  
18270198 Y.T.Meharenna, K.E.Slessor, S.M.Cavaignac, T.L.Poulos, and J.J.De Voss (2008).
The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin.
  J Biol Chem, 283, 10804-10812.
PDB codes: 3bdz 3be0
17534532 A.W.Munro, H.M.Girvan, and K.J.McLean (2007).
Variations on a (t)heme--novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamily.
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17598143 H.Yao, C.R.McCullough, A.D.Costache, P.K.Pullela, and D.S.Sem (2007).
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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17450550 J.Zheng, A.Altun, and W.Thiel (2007).
Common system setup for the entire catalytic cycle of cytochrome P450(cam) in quantum mechanical/molecular mechanical studies.
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17020766 C.W.Chiang, H.C.Yeh, L.H.Wang, and N.L.Chan (2006).
Crystal structure of the human prostacyclin synthase.
  J Mol Biol, 364, 266-274.
PDB code: 2iag
16500955 D.E.Prosser, Y.Guo, Z.Jia, and G.Jones (2006).
Structural motif-based homology modeling of CYP27A1 and site-directed mutational analyses affecting vitamin D hydroxylation.
  Biophys J, 90, 3389-3409.  
16793528 M.J.de Groot (2006).
Designing better drugs: predicting cytochrome P450 metabolism.
  Drug Discov Today, 11, 601-606.  
16328458 S.Todorovic, C.Jung, P.Hildebrandt, and D.H.Murgida (2006).
Conformational transitions and redox potential shifts of cytochrome P450 induced by immobilization.
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16873123 S.Y.Reece, J.M.Hodgkiss, J.Stubbe, and D.G.Nocera (2006).
Proton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology.
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15858263 F.Meilleur, M.T.Dauvergne, I.Schlichting, and D.A.Myles (2005).
Production and X-ray crystallographic analysis of fully deuterated cytochrome P450cam.
  Acta Crystallogr D Biol Crystallogr, 61, 539-544.
PDB codes: 1yrc 1yrd
15912546 F.Xu, S.G.Bell, J.Lednik, A.Insley, Z.Rao, and L.L.Wong (2005).
The heme monooxygenase cytochrome P450cam can be engineered to oxidize ethane to ethanol.
  Angew Chem Int Ed Engl, 44, 4029-4032.  
15617063 J.Mestres (2005).
Structure conservation in cytochromes P450.
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15880696 J.Nakazawa, J.Hagiwara, M.Mizuki, Y.Shimazaki, F.Tani, and Y.Naruta (2005).
Size-selective and reversible encapsulation of single small hydrocarbon molecules by a cavitand-porphyrin species.
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15854816 N.Bistolas, U.Wollenberger, C.Jung, and F.W.Scheller (2005).
Cytochrome P450 biosensors-a review.
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15912551 R.Murugan, and S.Mazumdar (2005).
Structure and redox properties of the haem centre in the C357M mutant of cytochrome P450cam.
  Chembiochem, 6, 1204-1211.  
15146488 D.L.Harris, J.Y.Park, L.Gruenke, and L.Waskell (2004).
Theoretical study of the ligand-CYP2B4 complexes: effect of structure on binding free energies and heme spin state.
  Proteins, 55, 895-914.  
15345570 F.J.Chartier, and M.Couture (2004).
Stability of the heme environment of the nitric oxide synthase from Staphylococcus aureus in the absence of pterin cofactor.
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15020591 H.M.Girvan, K.R.Marshall, R.J.Lawson, D.Leys, M.G.Joyce, J.Clarkson, W.E.Smith, M.R.Cheesman, and A.W.Munro (2004).
Flavocytochrome P450 BM3 mutant A264E undergoes substrate-dependent formation of a novel heme iron ligand set.
  J Biol Chem, 279, 23274-23286.  
15386621 M.Prudêncio, and M.Ubbink (2004).
Transient complexes of redox proteins: structural and dynamic details from NMR studies.
  J Mol Recognit, 17, 524-539.  
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.  
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.  
14688245 V.Schünemann, F.Lendzian, C.Jung, J.Contzen, A.L.Barra, S.G.Sligar, and A.X.Trautwein (2004).
Tyrosine radical formation in the reaction of wild type and mutant cytochrome P450cam with peroxy acids: a multifrequency EPR study of intermediates on the millisecond time scale.
  J Biol Chem, 279, 10919-10930.  
15258138 X.He, and P.R.de Montellano (2004).
Radical rebound mechanism in cytochrome P-450-catalyzed hydroxylation of the multifaceted radical clocks alpha- and beta-thujone.
  J Biol Chem, 279, 39479-39484.  
12586937 A.Karlsson, J.V.Parales, R.E.Parales, D.T.Gibson, H.Eklund, and S.Ramaswamy (2003).
Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron.
  Science, 299, 1039-1042.
PDB codes: 1o7g 1o7h 1o7m 1o7n 1o7p 1o7w
12831319 D.F.Lewis (2003).
P450 structures and oxidative metabolism of xenobiotics.
  Pharmacogenomics, 4, 387-395.  
12805387 G.M.Knudsen, C.R.Nishida, S.D.Mooney, and P.R.Ortiz de Montellano (2003).
Nitric-oxide synthase (NOS) reductase domain models suggest a new control element in endothelial NOS that attenuates calmodulin-dependent activity.
  J Biol Chem, 278, 31814-31824.  
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
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
12842870 T.Tosha, S.Yoshioka, S.Takahashi, K.Ishimori, H.Shimada, and I.Morishima (2003).
NMR study on the structural changes of cytochrome P450cam upon the complex formation with putidaredoxin. Functional significance of the putidaredoxin-induced structural changes.
  J Biol Chem, 278, 39809-39821.  
12081961 G.A.Roberts, G.Grogan, A.Greter, S.L.Flitsch, and N.J.Turner (2002).
Identification of a new class of cytochrome P450 from a Rhodococcus sp.
  J Bacteriol, 184, 3898-3908.  
12012432 J.H.Dawson, A.E.Pond, and M.P.Roach (2002).
H93G myoglobin cavity mutant as versatile template for modeling heme proteins: magnetic circular dichroism studies of thiolate- and imidazole-ligated complexes.
  Biopolymers, 67, 200-206.  
11922953 M.J.de Groot, and S.Ekins (2002).
Pharmacophore modeling of cytochromes P450.
  Adv Drug Deliv Rev, 54, 367-383.  
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.  
11922954 S.B.Kirton, C.A.Baxter, and M.J.Sutcliffe (2002).
Comparative modelling of cytochromes P450.
  Adv Drug Deliv Rev, 54, 385-406.  
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.  
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
11828481 M.A.Noordermeer, G.A.Veldink, and J.F.Vliegenthart (2001).
Fatty acid hydroperoxide lyase: a plant cytochrome p450 enzyme involved in wound healing and pest resistance.
  Chembiochem, 2, 494-504.  
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.  
11087371 C.Tetreau, M.Tourbez, and D.Lavalette (2000).
Conformational relaxation in hemoproteins: the cytochrome P-450cam case.
  Biochemistry, 39, 14219-14231.  
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
10698731 I.Schlichting, J.Berendzen, K.Chu, A.M.Stock, S.A.Maves, D.E.Benson, R.M.Sweet, D.Ringe, G.A.Petsko, and S.G.Sligar (2000).
The catalytic pathway of cytochrome p450cam at atomic resolution.
  Science, 287, 1615-1622.
PDB codes: 1dz4 1dz6 1dz8 1dz9
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
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.  
9888815 D.R.Davydov, G.Hui Bon Hoa, and J.A.Peterson (1999).
Dynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: comparison with P450cam and P450 2B4.
  Biochemistry, 38, 751-761.  
10557259 I.J.Dmochowski, B.R.Crane, J.J.Wilker, J.R.Winkler, and H.B.Gray (1999).
Optical detection of cytochrome P450 by sensitizer-linked substrates.
  Proc Natl Acad Sci U S A, 96, 12987-12990.
PDB code: 1qmq
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.  
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.  
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.
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9692324 F.Nastri, A.Lombardi, L.D.D'Andrea, M.Sanseverino, O.Maglio, and V.Pavone (1998).
Miniaturized hemoproteins.
  Biopolymers, 47, 5.  
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.  
9533688 W.Jentzen, J.G.Ma, and J.A.Shelnutt (1998).
Conservation of the conformation of the porphyrin macrocycle in hemoproteins.
  Biophys J, 74, 753-763.  
8993324 C.Di Primo, E.Deprez, S.G.Sligar, and G.Hui Bon Hoa (1997).
Origin of the photoacoustic signal in cytochrome P-450cam: role of the Arg186-Asp251-Lys178 bifurcated salt bridge.
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9201961 C.Mouro, C.Jung, A.Bondon, and G.Simonneaux (1997).
Comparative Fourier transform infrared studies of the secondary structure and the CO heme ligand environment in cytochrome P-450cam and cytochrome P-420cam.
  Biochemistry, 36, 8125-8134.  
9254625 C.Tétreau, C.Di Primo, R.Lange, H.Tourbez, and D.Lavalette (1997).
Dynamics of carbon monoxide binding with cytochromes P-450.
  Biochemistry, 36, 10262-10275.  
9283090 C.T.Migita, J.C.Salerno, B.S.Masters, P.Martasek, K.McMillan, and M.Ikeda-Saito (1997).
Substrate binding-induced changes in the EPR spectra of the ferrous nitric oxide complexes of neuronal nitric oxide synthase.
  Biochemistry, 36, 10987-10992.  
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.  
  9512922 M.D.Segall, M.C.Payne, S.W.Ellis, G.T.Tucker, and R.N.Boyes (1997).
Ab initio molecular modeling in the study of drug metabolism.
  Eur J Drug Metab Pharmacokinet, 22, 283-289.  
9268300 M.Holden, M.Mayhew, D.Bunk, A.Roitberg, and V.Vilker (1997).
Probing the interactions of putidaredoxin with redox partners in camphor P450 5-monooxygenase by mutagenesis of surface residues.
  J Biol Chem, 272, 21720-21725.  
9188703 N.Izadi, Y.Henry, J.Haladjian, M.E.Goldberg, C.Wandersman, M.Delepierre, and A.Lecroisey (1997).
Purification and characterization of an extracellular heme-binding protein, HasA, involved in heme iron acquisition.
  Biochemistry, 36, 7050-7057.  
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.  
9154922 V.Lounnas, and R.C.Wade (1997).
Exceptionally stable salt bridges in cytochrome P450cam have functional roles.
  Biochemistry, 36, 5402-5417.  
8988010 A.C.Gorren, B.M.List, A.Schrammel, E.Pitters, B.Hemmens, E.R.Werner, K.Schmidt, and B.Mayer (1996).
Tetrahydrobiopterin-free neuronal nitric oxide synthase: evidence for two identical highly anticooperative pteridine binding sites.
  Biochemistry, 35, 16735-16745.  
8654415 C.Jung, O.Ristau, H.Schulze, and S.G.Sligar (1996).
The CO stretching mode infrared spectrum of substrate-free cytochrome P-450cam-CO: the effect of solvent conditions, temperature, and pressure.
  Eur J Biochem, 235, 660-669.  
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Conformational dynamics in cytochrome P450-substrate interactions.
  Biochimie, 78, 695-699.  
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Structural changes in cytochrome P-450cam effected by the binding of the enantiomers (1R)-camphor and (1S)-camphor.
  Biochemistry, 35, 14127-14138.  
8673608 J.R.Cupp-Vickery, O.Han, C.R.Hutchinson, and T.L.Poulos (1996).
Substrate-assisted catalysis in cytochrome P450eryF.
  Nat Struct Biol, 3, 632-637.  
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.  
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.  
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.  
8605204 S.Modi, M.J.Paine, M.J.Sutcliffe, L.Y.Lian, W.U.Primrose, C.R.Wolf, and G.C.Roberts (1996).
A model for human cytochrome P450 2D6 based on homology modeling and NMR studies of substrate binding.
  Biochemistry, 35, 4540-4550.  
8612070 S.Modi, M.J.Sutcliffe, W.U.Primrose, L.Y.Lian, and G.C.Roberts (1996).
The catalytic mechanism of cytochrome P450 BM3 involves a 6 A movement of the bound substrate on reduction.
  Nat Struct Biol, 3, 414-417.  
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.  
8634279 V.Helms, E.Deprez, E.Gill, C.Barret, G.Hui Bon Hoa, and R.C.Wade (1996).
Improved binding of cytochrome P450cam substrate analogues designed to fill extra space in the substrate binding pocket.
  Biochemistry, 35, 1485-1499.  
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.  
7588807 C.Jung, G.Hui Bon Hoa, D.Davydov, E.Gill, and K.Heremans (1995).
Compressibility of the heme pocket of substrate analogue complexes of cytochrome P-450cam-CO. The effect of hydrostatic pressure on the Soret band.
  Eur J Biochem, 233, 600-606.  
  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.  
7749919 J.R.Cupp-Vickery, and T.L.Poulos (1995).
Structure of cytochrome P450eryF involved in erythromycin biosynthesis.
  Nat Struct Biol, 2, 144-153.
PDB code: 1oxa
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.  
8519982 V.Helms, and R.C.Wade (1995).
Thermodynamics of water mediating protein-ligand interactions in cytochrome P450cam: a molecular dynamics study.
  Biophys J, 69, 810-824.  
7721770 W.D.Tian, A.V.Wells, P.M.Champion, C.Di Primo, N.Gerber, and S.G.Sligar (1995).
Measurements of CO geminate recombination in cytochromes P450 and P420.
  J Biol Chem, 270, 8673-8679.  
7922023 H.Li, and T.L.Poulos (1994).
Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures.
  Structure, 2, 461-464.  
7846029 J.R.Cupp-Vickery, H.Li, and T.L.Poulos (1994).
Preliminary crystallographic analysis of an enzyme involved in erythromycin biosynthesis: cytochrome P450eryF.
  Proteins, 20, 197-201.  
  8376348 J.D.Ropp, I.C.Gunsalus, and S.G.Sligar (1993).
Cloning and expression of a member of a new cytochrome P-450 family: cytochrome P-450lin (CYP111) from Pseudomonas incognita.
  J Bacteriol, 175, 6028-6037.  
8464908 K.Warncke, and P.L.Dutton (1993).
Experimental resolution of the free energies of aqueous solvation contributions to ligand-protein binding: quinone-QA site interactions in the photosynthetic reaction center protein.
  Proc Natl Acad Sci U S A, 90, 2920-2924.  
8218905 L.Banci, I.Bertini, L.D.Eltis, and R.Pierattelli (1993).
Spectroscopic characterization of a newly isolated cytochrome P450 from Rhodococcus rhodochrous.
  Biophys J, 65, 806-813.  
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.  
1608967 S.S.Boddupalli, C.A.Hasemann, K.G.Ravichandran, J.Y.Lu, E.J.Goldsmith, J.Deisenhofer, and J.A.Peterson (1992).
Crystallization 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.
  Proc Natl Acad Sci U S A, 89, 5567-5571.  
1749772 M.D.Paulsen, and R.L.Ornstein (1991).
A 175-psec molecular dynamics simulation of camphor-bound cytochrome P-450cam.
  Proteins, 11, 184-204.  
1852787 R.E.White (1991).
The involvement of free radicals in the mechanisms of monooxygenases.
  Pharmacol Ther, 49, 21-42.  
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.  
2405436 D.E.Ryan, and W.Levin (1990).
Purification and characterization of hepatic microsomal cytochrome P-450.
  Pharmacol Ther, 45, 153-239.  
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.  
2213064 R.C.Wade (1990).
Solvation of the active site of cytochrome P450-cam.
  J Comput Aided Mol Des, 4, 199-204.  
  2683413 G.G.Gibson (1989).
Comparative aspects of the mammalian cytochrome P450 IV gene family.
  Xenobiotica, 19, 1123-1148.  
2753040 H.Langen, T.Epprecht, M.Linden, T.Hehlgans, B.Gutte, and H.R.Buser (1989).
Rapid partial degradation of DDT by a cytochrome P-450 model system.
  Eur J Biochem, 182, 727-735.  
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.  
2854395 D.L.Rousseau, M.Sassaroli, Y.C.Ching, and S.Dasgupta (1988).
The role of water near cytochrome a in cytochrome c oxidase.
  Ann N Y Acad Sci, 550, 223-237.  
3278179 J.P.Tollenaere, and P.A.Janssen (1988).
Conformational analysis and computer graphics in drug research.
  Med Res Rev, 8, 1.  
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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