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Oxidoreductase PDB id
1dz9
Jmol
Contents
Protein chains
404 a.a. *
Ligands
HEM-__O
CAM ×2
TRS
HEM
Metals
__K ×3
Waters ×709
* Residue conservation analysis
PDB id:
1dz9
Name: Oxidoreductase
Title: Putative oxo complex of p450cam from pseudomonas putida
Structure: Cytochrome p450-cam. Chain: a, b. Engineered: yes. Other_details: oxygen bound to heme iron. Heme attached via cys357
Source: Pseudomonas putida. Organism_taxid: 303. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.9Å     R-factor:   0.177     R-free:   0.248
Authors: I.Schlichting,J.Berendzen,K.Chu,A.M.Stock,S.A.Maves, D.E.Benson,R.M.Sweet,D.Ringe,G.A.Petsko,S.G.Sligar
Key ref:
I.Schlichting et al. (2000). The catalytic pathway of cytochrome p450cam at atomic resolution. Science, 287, 1615-1622. PubMed id: 10698731 DOI: 10.1126/science.287.5458.1615
Date:
18-Feb-00     Release date:   30-Mar-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00183  (CPXA_PSEPU) -  Camphor 5-monooxygenase
Seq:
Struc: 		415 a.a.
405 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.1.14.15.1  - Camphor 5-monooxygenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: +-camphor + putidaredoxin + O2 = +-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
(+)-camphor
Bound ligand (Het Group name = CAM)
corresponds exactly 		+ putidaredoxin
 + O(2)
 = (+)-exo-5-hydroxycamphor
 + oxidized putidaredoxin
 + H(2)O
      Cofactor: Heme-thiolate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     oxidation reduction   1 term 
  Biochemical function     electron carrier activity     7 terms  

 

 
    reference    
 
 
DOI no: 10.1126/science.287.5458.1615 Science 287:1615-1622 (2000)
PubMed id: 10698731  
 
 
The catalytic pathway of cytochrome p450cam at atomic resolution.
I.Schlichting, J.Berendzen, K.Chu, A.M.Stock, S.A.Maves, D.E.Benson, R.M.Sweet, D.Ringe, G.A.Petsko, S.G.Sligar.
 
  ABSTRACT  
 
Members of the cytochrome P450 superfamily catalyze the addition of molecular oxygen to nonactivated hydrocarbons at physiological temperature-a reaction that requires high temperature to proceed in the absence of a catalyst. Structures were obtained for three intermediates in the hydroxylation reaction of camphor by P450cam with trapping techniques and cryocrystallography. The structure of the ferrous dioxygen adduct of P450cam was determined with 0.91 angstrom wavelength x-rays; irradiation with 1.5 angstrom x-rays results in breakdown of the dioxygen molecule to an intermediate that would be consistent with an oxyferryl species. The structures show conformational changes in several important residues and reveal a network of bound water molecules that may provide the protons needed for the reaction.
 
  Selected figure(s)  
 
Figure 4.
Fig. 4. (A) Stereoview of comparison of the camphor complexes of ferrous (dark gray and dark blue water molecules) and ferrous dioxygen-bound (light gray and cyan water molecules) P450. Upon oxygen binding, camphor is displaced, two new water molecules bind, the backbone carbonyl group of Asp251 flips, and the backbone amide of Thr252 rotates as does its side chain. (B) The interactions of the two new water molecules and the water chain extending from the first new water molecule to Glu366. Figures were generated with Bobscript (34) and Raster 3D (35). 		Figure 6.
Fig. 6. Stereoviews of comparison of the structures of the ferric camphor complex of wild-type P450 (A) and the D251N mutant (PDB entry 6CP4) (B). As described in the text, flipping of the Asp251-Thr252 backbone, required for stabilization of a presumably catalytic water molecule, is energetically supported by a new hydrogen bond between the carbonyl oxygen of Asp251 and the side-chain amide of Asn255. However, in the mutant enzyme, the latter group is involved in a hydrogen bond with the side-chain carbonyl of the mutated residue Asn251. We predict that this reduces the stabilization of the water molecule and thus causes the reduced affinity. Figures were generated with Bobscript (34) and Raster 3D (35).
 
  The above figures are reprinted by permission from the AAAs: Science (2000, 287, 1615-1622) copyright 2000.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21525643 A.M.Orville, R.Buono, M.Cowan, A.Héroux, G.Shea-McCarthy, D.K.Schneider, J.M.Skinner, M.J.Skinner, D.Stoner-Ma, and R.M.Sweet (2011).
Correlated single-crystal electronic absorption spectroscopy and X-ray crystallography at NSLS beamline X26-C.
  J Synchrotron Radiat, 18, 358-366.  
21525640 D.H.Juers, and M.Weik (2011).
Similarities and differences in radiation damage at 100 K versus 160 K in a crystal of thermolysin.
  J Synchrotron Radiat, 18, 329-337.  
21384946 H.J.Kulik, and N.Marzari (2011).
Transition-metal dioxides: A case for the intersite term in Hubbard-model functionals.
  J Chem Phys, 134, 094103.  
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
21308129 O.Shoji, and Y.Watanabe (2011).
Design of H2O2-dependent oxidation catalyzed by hemoproteins.
  Metallomics, 3, 379-388.  
21356195 R.Brandman, J.N.Lampe, Y.Brandman, and P.R.de Montellano (2011).
Active-site residues move independently from the rest of the protein in a 200 ns molecular dynamics simulation of cytochrome P450 CYP119.
  Arch Biochem Biophys, 509, 127-132.  
21525644 R.L.Owen, B.A.Yorke, J.A.Gowdy, and A.R.Pearson (2011).
Revealing low-dose radiation damage using single-crystal spectroscopy.
  J Synchrotron Radiat, 18, 367-373.  
21160515 S.Fukuzumi, T.Kishi, H.Kotani, Y.M.Lee, and W.Nam (2011).
Highly efficient photocatalytic oxygenation reactions using water as an oxygen source.
  Nat Chem, 3, 38-41.  
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 .
  Biochemistry, 50, 693-703.  
20361237 A.Tarcsay, R.Kiss, and G.M.Keseru (2010).
Site of metabolism prediction on cytochrome P450 2C9: a knowledge-based docking approach.
  J Comput Aided Mol Des, 24, 399-408.  
20386942 B.R.Goblirsch, B.R.Streit, J.L.Dubois, and C.M.Wilmot (2010).
Structural features promoting dioxygen production by Dechloromonas aromatica chlorite dismutase.
  J Biol Inorg Chem, 15, 879-888.
PDB codes: 3m2q 3m2s 3q08 3q09
21107372 C.Cavazza, C.Bochot, P.Rousselot-Pailley, P.Carpentier, M.V.Cherrier, L.Martin, C.Marchi-Delapierre, J.C.Fontecilla-Camps, and S.Ménage (2010).
Crystallographic snapshots of the reaction of aromatic C-H with O(2) catalysed by a protein-bound iron complex.
  Nat Chem, 2, 1069-1076.
PDB codes: 3mvw 3mvx 3mvy 3mvz 3mw0 3mz9 3mzb
21068844 C.Yi, G.Jia, G.Hou, Q.Dai, W.Zhang, G.Zheng, X.Jian, C.G.Yang, Q.Cui, and C.He (2010).
Iron-catalysed oxidation intermediates captured in a DNA repair dioxygenase.
  Nature, 468, 330-333.  
20387782 D.Fishelovitch, S.Shaik, H.J.Wolfson, and R.Nussinov (2010).
How does the reductase help to regulate the catalytic cycle of cytochrome P450 3A4 using the conserved water channel?
  J Phys Chem B, 114, 5964-5970.  
20382986 E.F.Garman (2010).
Radiation damage in macromolecular crystallography: what is it and why should we care?
  Acta Crystallogr D Biol Crystallogr, 66, 339-351.  
20801213 E.Sedlák, M.Fabian, N.C.Robinson, and A.Musatov (2010).
Ferricytochrome c protects mitochondrial cytochrome c oxidase against hydrogen peroxide-induced oxidative damage.
  Free Radic Biol Med, 49, 1574-1581.  
19923211 G.I.Lepesheva, H.W.Park, T.Y.Hargrove, B.Vanhollebeke, Z.Wawrzak, J.M.Harp, M.Sundaramoorthy, W.D.Nes, E.Pays, M.Chaudhuri, F.Villalta, and M.R.Waterman (2010).
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  J Biol Chem, 285, 1773-1780.
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21071661 J.Rittle, and M.T.Green (2010).
Cytochrome P450 compound I: capture, characterization, and C-H bond activation kinetics.
  Science, 330, 933-937.  
20148224 K.Duerr, J.Olah, R.Davydov, M.Kleimann, J.Li, N.Lang, R.Puchta, E.Hübner, T.Drewello, J.N.Harvey, N.Jux, and I.Ivanović-Burmazović (2010).
Studies on an iron(iii)-peroxo porphyrin. Iron(III)-peroxo or iron(II)-superoxo?
  Dalton Trans, 39, 2049-2056.  
20498847 K.M.Manoj, A.Baburaj, B.Ephraim, F.Pappachan, P.P.Maviliparambathu, U.K.Vijayan, S.V.Narayanan, K.Periasamy, E.A.George, and L.T.Mathew (2010).
Explaining the atypical reaction profiles of heme enzymes with a novel mechanistic hypothesis and kinetic treatment.
  PLoS One, 5, e10601.  
20059399 L.M.Blank, B.E.Ebert, K.Buehler, and B.Bühler (2010).
Redox biocatalysis and metabolism: molecular mechanisms and metabolic network analysis.
  Antioxid Redox Signal, 13, 349-394.  
20837547 M.M.Mbughuni, M.Chakrabarti, J.A.Hayden, E.L.Bominaar, M.P.Hendrich, E.Münck, and J.D.Lipscomb (2010).
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  Proc Natl Acad Sci U S A, 107, 16788-16793.  
20382998 M.Schiltz, and G.Bricogne (2010).
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  Acta Crystallogr D Biol Crystallogr, 66, 447-457.  
20944242 M.Warkentin, and R.E.Thorne (2010).
Glass transition in thaumatin crystals revealed through temperature-dependent radiation-sensitivity measurements.
  Acta Crystallogr D Biol Crystallogr, 66, 1092-1100.  
20382997 M.Weik, and J.P.Colletier (2010).
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  Acta Crystallogr D Biol Crystallogr, 66, 437-446.  
19947890 N.Shakunthala (2010).
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  Expert Opin Drug Metab Toxicol, 6, 1.  
21070940 P.Carpentier, A.Royant, M.Weik, and D.Bourgeois (2010).
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  Structure, 18, 1410-1419.
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19769330 P.R.Ortiz de Montellano (2010).
Hydrocarbon hydroxylation by cytochrome P450 enzymes.
  Chem Rev, 110, 932-948.  
20485834 S.Friedle, E.Reisner, and S.J.Lippard (2010).
Current challenges of modeling diiron enzyme active sites for dioxygen activation by biomimetic synthetic complexes.
  Chem Soc Rev, 39, 2768-2779.  
21071657 S.G.Sligar (2010).
Chemistry. Glimpsing the critical intermediate in cytochrome P450 oxidations.
  Science, 330, 924-925.  
20164644 S.Westenhoff, E.Nazarenko, E.Malmerberg, J.Davidsson, G.Katona, and R.Neutze (2010).
Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches.
  Acta Crystallogr A, 66, 207-219.  
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.  
20950270 W.Yang, S.G.Bell, H.Wang, W.Zhou, M.Bartlam, L.L.Wong, and Z.Rao (2010).
The structure of CYP101D2 unveils a potential path for substrate entry into the active site.
  Biochem J, 433, 85-93.
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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.
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19438234 A.Dey, Y.Jiang, P.Ortiz de Montellano, K.O.Hodgson, B.Hedman, and E.I.Solomon (2009).
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  J Am Chem Soc, 131, 7869-7878.  
19133805 A.M.Orville, G.T.Lountos, S.Finnegan, G.Gadda, and R.Prabhakar (2009).
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  Biochemistry, 48, 720-728.  
  19652348 B.R.Goblirsch, B.R.Streit, J.L.DuBois, and C.M.Wilmot (2009).
Crystallization and preliminary X-ray diffraction of chlorite dismutase from Dechloromonas aromatica RCB.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 818-821.  
19293375 C.Aldag, I.A.Gromov, I.García-Rubio, K.von Koenig, I.Schlichting, B.Jaun, and D.Hilvert (2009).
Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine.
  Proc Natl Acad Sci U S A, 106, 5481-5486.
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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.
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19327368 E.K.Asciutto, J.D.Madura, S.S.Pochapsky, B.OuYang, and T.C.Pochapsky (2009).
Structural and dynamic implications of an effector-induced backbone amide cis-trans isomerization in cytochrome P450cam.
  J Mol Biol, 388, 801-814.  
19187034 H.C.Yeh, G.J.Gerfen, J.S.Wang, A.L.Tsai, and L.H.Wang (2009).
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  Biochemistry, 48, 917-928.  
19605359 H.Zhang, C.Kenaan, D.Hamdane, G.H.Hoa, and P.F.Hollenberg (2009).
Effect of conformational dynamics on substrate recognition and specificity as probed by the introduction of a de novo disulfide bond into cytochrome P450 2B1.
  J Biol Chem, 284, 25678-25686.  
  19193991 K.Sakurai, H.Shimada, T.Hayashi, and T.Tsukihara (2009).
Substrate binding induces structural changes in cytochrome P450cam.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 80-83.
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19360792 L.F.Pacios, V.M.Campos, I.Merino, and L.Gómez (2009).
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  J Comput Chem, 30, 2420-2432.  
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QM/MM Simulation on P450 BM3 Enzyme Catalysis Mechanism.
  J Chem Theory Comput, 5, 1421-1431.  
19345605 M.T.Green (2009).
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  Curr Opin Chem Biol, 13, 84-88.  
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  J Lipid Res, 50, 1015-1038.  
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  Biochemistry, 48, 9801-9809.  
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  Chem Rev, 109, 1793-1899.  
19347895 S.P.de Visser, L.Tahsini, and W.Nam (2009).
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  Chemistry, 15, 5577-5587.  
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  Chemistry, 15, 4464-4473.  
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  Dalton Trans, 0, 8111-8116.  
18513977 B.OuYang, S.S.Pochapsky, M.Dang, and T.C.Pochapsky (2008).
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  Structure, 16, 916-923.  
18600471 D.Hamdane, H.Zhang, and P.Hollenberg (2008).
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  Photosynth Res, 98, 657-666.  
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.  
19040328 D.R.Davydov, and J.R.Halpert (2008).
Allosteric P450 mechanisms: multiple binding sites, multiple conformers or both?
  Expert Opin Drug Metab Toxicol, 4, 1523-1535.  
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Low-frequency dynamics of Caldariomyces fumago chloroperoxidase probed by femtosecond coherence spectroscopy.
  Biochemistry, 47, 5156-5167.  
18196297 H.Hirao, K.B.Cho, and S.Shaik (2008).
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  J Biol Inorg Chem, 13, 521-530.  
18092942 J.C.Rasaiah, S.Garde, and G.Hummer (2008).
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  Annu Rev Phys Chem, 59, 713-740.  
18701720 J.P.Colletier, D.Bourgeois, B.Sanson, D.Fournier, J.L.Sussman, I.Silman, and M.Weik (2008).
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  Proc Natl Acad Sci U S A, 105, 11742-11747.
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18180042 M.Freindorf, Y.Shao, J.Kong, and T.R.Furlani (2008).
Combined QM/MM calculations of active-site vibrations in binding process of P450cam to putidaredoxin.
  J Inorg Biochem, 102, 427-432.  
18161730 M.J.Cryle, and J.J.De Voss (2008).
The role of the conserved threonine in P450 BM3 oxygen activation: substrate-determined hydroxylation activity of the Thr268Ala mutant.
  Chembiochem, 9, 261-266.  
18446388 M.Makarska, and G.Pratviel (2008).
Long-range charge transport through double-stranded DNA mediated by manganese or iron porphyrins.
  J Biol Inorg Chem, 13, 973-979.  
18700729 R.Davydov, R.Razeghifard, S.C.Im, L.Waskell, and B.M.Hoffman (2008).
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  Biochemistry, 47, 9661-9666.  
19082087 R.L.Shook, and A.S.Borovik (2008).
The effects of hydrogen bonds on metal-mediated O2 activation and related processes.
  Chem Commun (Camb), 0, 6095-6107.  
18844316 T.K.Yanai, and S.Mori (2008).
Density functional studies on thromboxane biosynthesis: mechanism and role of the heme-thiolate system.
  Chem Asian J, 3, 1900-1911.  
18273651 T.Spolitak, J.H.Dawson, and D.P.Ballou (2008).
Replacement of tyrosine residues by phenylalanine in cytochrome P450cam alters the formation of Cpd II-like species in reactions with artificial oxidants.
  J Biol Inorg Chem, 13, 599-611.  
18445553 V.Guallar, and F.Wallrapp (2008).
Mapping protein electron transfer pathways with QM/MM methods.
  J R Soc Interface, 5, S233-S239.  
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.
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17404234 A.Arcovito, M.Benfatto, M.Cianci, S.S.Hasnain, K.Nienhaus, G.U.Nienhaus, C.Savino, R.W.Strange, B.Vallone, and S.Della Longa (2007).
X-ray structure analysis of a metalloprotein with enhanced active-site resolution using in situ x-ray absorption near edge structure spectroscopy.
  Proc Natl Acad Sci U S A, 104, 6211-6216.
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17387527 A.R.Shaikh, E.Broclawik, H.Tsuboi, M.Koyama, A.Endou, H.Takaba, M.Kubo, C.A.Del Carpio, and A.Miyamoto (2007).
Oxidation mechanism in the metabolism of (S)-N-[1-(3-morpholin-4-ylphenyl)ethyl]-3-phenylacrylamide on oxyferryl active site in CYP3A4 Cytochrome: DFT modeling.
  J Mol Model, 13, 851-860.  
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.
  Nat Prod Rep, 24, 585-609.  
  18379640 I.G.Denisov, D.C.Victoria, and S.G.Sligar (2007).
Cryoradiolytic reduction of heme proteins: Maximizing dose dependent yield.
  Radiat Phys Chem Oxf Engl 1993, 76, 714-721.  
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.
  J Comput Chem, 28, 2147-2158.  
18075575 K.Henzler-Wildman, and D.Kern (2007).
Dynamic personalities of proteins.
  Nature, 450, 964-972.  
17190816 K.Kühnel, E.Derat, J.Terner, S.Shaik, and I.Schlichting (2007).
Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes.
  Proc Natl Acad Sci U S A, 104, 99.
PDB code: 2j5m
18220563 L.Jia, and X.Liu (2007).
The conduct of drug metabolism studies considered good practice (II): in vitro experiments.
  Curr Drug Metab, 8, 822-829.  
17686967 L.Wei, C.W.Locuson, and T.S.Tracy (2007).
Polymorphic variants of CYP2C9: mechanisms involved in reduced catalytic activity.
  Mol Pharmacol, 72, 1280-1288.  
17318598 M.A.Carrondo, I.Bento, P.M.Matias, and P.F.Lindley (2007).
Crystallographic evidence for dioxygen interactions with iron proteins.
  J Biol Inorg Chem, 12, 429-442.  
17704563 M.C.Corbett, M.J.Latimer, T.L.Poulos, I.F.Sevrioukova, K.O.Hodgson, and B.Hedman (2007).
Photoreduction of the active site of the metalloprotein putidaredoxin by synchrotron radiation.
  Acta Crystallogr D Biol Crystallogr, 63, 951-960.  
17473016 M.J.Borrok, L.L.Kiessling, and K.T.Forest (2007).
Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures.
  Protein Sci, 16, 1032-1041.
PDB codes: 2fvy 2fw0
17461587 P.J.Mak, I.G.Denisov, D.Victoria, T.M.Makris, T.Deng, S.G.Sligar, and J.R.Kincaid (2007).
Resonance Raman detection of the hydroperoxo intermediate in the cytochrome P450 enzymatic cycle.
  J Am Chem Soc, 129, 6382-6383.  
17534529 S.Shaik, H.Hirao, and D.Kumar (2007).
Reactivity patterns of cytochrome P450 enzymes: multifunctionality of the active species, and the two states-two oxidants conundrum.
  Nat Prod Rep, 24, 533-552.  
17881827 V.de Serrano, Z.Chen, M.F.Davis, and S.Franzen (2007).
X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned from Amphitrite ornata.
  Acta Crystallogr D Biol Crystallogr, 63, 1094-1101.
PDB codes: 2qfk 2qfn
16788908 A.Altun, S.Shaik, and W.Thiel (2006).
Systematic QM/MM investigation of factors that affect the cytochrome P450-catalyzed hydrogen abstraction of camphor.
  J Comput Chem, 27, 1324-1337.  
16551096 A.Altun, V.Guallar, R.A.Friesner, S.Shaik, and W.Thiel (2006).
The effect of heme environment on the hydrogen abstraction reaction of camphor in P450cam catalysis: a QM/MM study.
  J Am Chem Soc, 128, 3924-3925.  
17149482 D.E.Bikiel, L.Boechi, L.Capece, A.Crespo, P.M.De Biase, S.Di Lella, M.C.González Lebrero, M.A.Martí, A.D.Nadra, L.L.Perissinotti, D.A.Scherlis, and D.A.Estrin (2006).
Modeling heme proteins using atomistic simulations.
  Phys Chem Chem Phys, 8, 5611-5628.  
16804678 H.Li, J.Igarashi, J.Jamal, W.Yang, and T.L.Poulos (2006).
Structural studies of constitutive nitric oxide synthases with diatomic ligands bound.
  J Biol Inorg Chem, 11, 753-768.
PDB codes: 2g6h 2g6i 2g6j 2g6k 2g6l 2g6m 2g6n 2g6o
16477023 H.Sugimoto, S.Oda, T.Otsuki, T.Hino, T.Yoshida, and Y.Shiro (2006).
Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase.
  Proc Natl Acad Sci U S A, 103, 2611-2616.
PDB codes: 2d0t 2d0u
16519512 J.Qin, R.Perera, L.L.Lovelace, J.H.Dawson, and L.Lebioda (2006).
Structures of thiolate- and carboxylate-ligated ferric H93G myoglobin: models for cytochrome P450 and for oxyanion-bound heme proteins.
  Biochemistry, 45, 3170-3177.
PDB codes: 2evk 2evp
17047872 J.Zurek, N.Foloppe, J.N.Harvey, and A.J.Mulholland (2006).
Mechanisms of reaction in cytochrome P450: Hydroxylation of camphor in P450cam.
  Org Biomol Chem, 4, 3931-3937.  
16432511 L.Jia, P.E.Noker, L.Coward, G.S.Gorman, M.Protopopova, and J.E.Tomaszewski (2006).
Interspecies pharmacokinetics and in vitro metabolism of SQ109.
  Br J Pharmacol, 147, 476-485.  
16548516 L.Rui, S.S.Pochapsky, and T.C.Pochapsky (2006).
Comparison of the complexes formed by cytochrome P450cam with cytochrome b5 and putidaredoxin, two effectors of camphor hydroxylase activity.
  Biochemistry, 45, 3887-3897.  
16777962 S.Eswaramoorthy, J.B.Bonanno, S.K.Burley, and S.Swaminathan (2006).
Mechanism of action of a flavin-containing monooxygenase.
  Proc Natl Acad Sci U S A, 103, 9832-9837.
PDB codes: 1vqw 2gv8 2gvc
16955357 T.Mouri, N.Kamiya, and M.Goto (2006).
Increasing the catalytic performance of a whole cell biocatalyst harboring a cytochrome p450cam system by stabilization of an electron transfer component.
  Biotechnol Lett, 28, 1509-1513.  
16862439 V.R.Dodhia, A.Fantuzzi, and G.Gilardi (2006).
Engineering human cytochrome P450 enzymes into catalytically self-sufficient chimeras using molecular Lego.
  J Biol Inorg Chem, 11, 903-916.  
17002293 V.Y.Kuznetsov, T.L.Poulos, and I.F.Sevrioukova (2006).
Putidaredoxin-to-cytochrome P450cam electron transfer: differences between the two reductive steps required for catalysis.
  Biochemistry, 45, 11934-11944.  
17083959 X.Ding, B.F.Rasmussen, G.A.Petsko, and D.Ringe (2006).
Direct crystallographic observation of an acyl-enzyme intermediate in the elastase-catalyzed hydrolysis of a peptidyl ester substrate: Exploiting the "glass transition" in protein dynamics.
  Bioorg Chem, 34, 410-423.  
15942729 A.Karlsson, J.V.Parales, R.E.Parales, D.T.Gibson, H.Eklund, and S.Ramaswamy (2005).
NO binding to naphthalene dioxygenase.
  J Biol Inorg Chem, 10, 483-489.
PDB codes: 1uuv 1uuw
15812779 A.Oda, N.Yamaotsu, and S.Hirono (2005).
New AMBER force field parameters of heme iron for cytochrome P450s determined by quantum chemical calculations of simplified models.
  J Comput Chem, 26, 818-826.  
15720389 B.Sielaff, and J.R.Andreesen (2005).
Kinetic and binding studies with purified recombinant proteins ferredoxin reductase, ferredoxin and cytochrome P450 comprising the morpholine mono-oxygenase from Mycobacterium sp. strain HE5.
  FEBS J, 272, 1148-1159.  
16129597 D.Bourgeois, and A.Royant (2005).
Advances in kinetic protein crystallography.
  Curr Opin Struct Biol, 15, 538-547.  
15723206 D.Kumar, S.P.de Visser, P.K.Sharma, E.Derat, and S.Shaik (2005).
The intrinsic axial ligand effect on propene oxidation by horseradish peroxidase versus cytochrome P450 enzymes.
  J Biol Inorg Chem, 10, 181-189.  
16046535 H.P.Lerch, R.Rigler, and A.S.Mikhailov (2005).
Functional conformational motions in the turnover cycle of cholesterol oxidase.
  Proc Natl Acad Sci U S A, 102, 10807-10812.  
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.  
16211539 J.L.Banks, H.S.Beard, Y.Cao, A.E.Cho, W.Damm, R.Farid, A.K.Felts, T.A.Halgren, D.T.Mainz, J.R.Maple, R.Murphy, D.M.Philipp, M.P.Repasky, L.Y.Zhang, B.J.Berne, R.A.Friesner, E.Gallicchio, and R.M.Levy (2005).
Integrated Modeling Program, Applied Chemical Theory (IMPACT).
  J Comput Chem, 26, 1752-1780.  
15884940 J.Y.Wei, T.C.Pochapsky, and S.S.Pochapsky (2005).
Detection of a high-barrier conformational change in the active site of cytochrome P450cam upon binding of putidaredoxin.
  J Am Chem Soc, 127, 6974-6976.  
16103362 J.Yano, J.Kern, K.D.Irrgang, M.J.Latimer, U.Bergmann, P.Glatzel, Y.Pushkar, J.Biesiadka, B.Loll, K.Sauer, J.Messinger, A.Zouni, and V.K.Yachandra (2005).
X-ray damage to the Mn4Ca complex in single crystals of photosystem II: a case study for metalloprotein crystallography.
  Proc Natl Acad Sci U S A, 102, 12047-12052.  
16275918 K.L.Stone, R.K.Behan, and M.T.Green (2005).
X-ray absorption spectroscopy of chloroperoxidase compound I: Insight into the reactive intermediate of P450 chemistry.
  Proc Natl Acad Sci U S A, 102, 16563-16565.  
16269539 M.D.Collins, G.Hummer, M.L.Quillin, B.W.Matthews, and S.M.Gruner (2005).
Cooperative water filling of a nonpolar protein cavity observed by high-pressure crystallography and simulation.
  Proc Natl Acad Sci U S A, 102, 16668-16671.
PDB codes: 2b6w 2b6x 2b6y 2b6z 2b70 2b72 2b73 2b74 2b75 2oe4
15602754 M.R.Bukowski, H.L.Halfen, T.A.van den Berg, J.A.Halfen, and L.Que (2005).
Spin-state rationale for the peroxo-stabilizing role of the thiolate ligand in superoxide reductase.
  Angew Chem Int Ed Engl, 44, 584-587.  
15796706 R.A.Friesner, and V.Guallar (2005).
Ab initio quantum chemical and mixed quantum mechanics/molecular mechanics (QM/MM) methods for studying enzymatic catalysis.
  Annu Rev Phys Chem, 56, 389-427.  
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.  
16234928 R.Silaghi-Dumitrescu, and C.E.Cooper (2005).
Transient species involved in catalytic dioxygen/peroxide activation by hemoproteins: possible involvement of protonated Compound I species.
  Dalton Trans, 0, 3477-3482.  
15651036 S.B.Kirton, C.W.Murray, M.L.Verdonk, and R.D.Taylor (2005).
Prediction of binding modes for ligands in the cytochromes P450 and other heme-containing proteins.
  Proteins, 58, 836-844.  
16234926 S.H.Kim, T.C.Yang, R.Perera, S.Jin, T.A.Bryson, M.Sono, R.Davydov, J.H.Dawson, and B.M.Hoffman (2005).
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.
  Dalton Trans, 0, 3464-3469.  
15832445 W.M.Atkins (2005).
Non-Michaelis-Menten kinetics in cytochrome P450-catalyzed reactions.
  Annu Rev Pharmacol Toxicol, 45, 291-310.  
15849199 X.He, M.J.Cryle, J.J.De Voss, and P.R.de Montellano (2005).
Calibration of the channel that determines the omega-hydroxylation regiospecificity of cytochrome P4504A1: catalytic oxidation of 12-HALODOdecanoic acids.
  J Biol Chem, 280, 22697-22705.  
15802473 X.Shan, and L.Que (2005).
Intermediates in the oxygenation of a nonheme diiron(II) complex, including the first evidence for a bound superoxo species.
  Proc Natl Acad Sci U S A, 102, 5340-5345.  
16155883 Y.K.Choe, and S.Nagase (2005).
Effect of the axial cysteine ligand on the electronic structure and reactivity of high-valent iron(IV) oxo-porphyrins (Compound I): a theoretical study.
  J Comput Chem, 26, 1600-1611.  
15057279 A.Rozhkova, C.U.Stirnimann, P.Frei, U.Grauschopf, R.Brunisholz, M.G.Grütter, G.Capitani, and R.Glockshuber (2004).
Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.
  EMBO J, 23, 1709-1719.
PDB codes: 1se1 1vrs
15546978 B.J.Bahnson (2004).
An atomic-resolution mechanism of 3-hydroxy-3-methylglutaryl-CoA synthase.
  Proc Natl Acad Sci U S A, 101, 16399-16400.  
15224385 H.Matter, and P.Kotsonis (2004).
Biology and chemistry of the inhibition of nitric oxide synthases by pteridine-derivatives as therapeutic agents.
  Med Res Rev, 24, 662-684.  
15062772 I.Matsunaga, and Y.Shiro (2004).
Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes.
  Curr Opin Chem Biol, 8, 127-132.  
15333928 J.Wang, and S.E.Ealick (2004).
Observation of time-resolved structural changes by linear interpolation of highly redundant X-ray diffraction data.
  Acta Crystallogr D Biol Crystallogr, 60, 1579-1585.  
15339813 K.Nilsson, H.P.Hersleth, T.H.Rod, K.K.Andersson, and U.Ryde (2004).
The protonation status of compound II in myoglobin, studied by a combination of experimental data and quantum chemical calculations: quantum refinement.
  Biophys J, 87, 3437-3447.  
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
15159561 M.Schiltz, P.Dumas, E.Ennifar, C.Flensburg, W.Paciorek, C.Vonrhein, and G.Bricogne (2004).
Phasing in the presence of severe site-specific radiation damage through dose-dependent modelling of heavy atoms.
  Acta Crystallogr D Biol Crystallogr, 60, 1024-1031.  
15041745 M.Schmidt, R.Pahl, V.Srajer, S.Anderson, Z.Ren, H.Ihee, S.Rajagopal, and K.Moffat (2004).
Protein kinetics: structures of intermediates and reaction mechanism from time-resolved x-ray data.
  Proc Natl Acad Sci U S A, 101, 4799-4804.
PDB codes: 1s4r 1s4s
15111430 M.Weik, X.Vernede, A.Royant, and D.Bourgeois (2004).
Temperature derivative fluorescence spectroscopy as a tool to study dynamical changes in protein crystals.
  Biophys J, 86, 3176-3185.  
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.  
15560776 P.Hlavica (2004).
Models and mechanisms of O-O bond activation by cytochrome P450. A critical assessment of the potential role of multiple active intermediates in oxidative catalysis.
  Eur J Biochem, 271, 4335-4360.  
15648140 P.Pantu, S.Pabchanda, and J.Limtrakul (2004).
Theoretical investigation of the selective oxidation of methane to methanol on nanostructured fe-zSM-5 by the ONIOM method.
  Chemphyschem, 5, 1901-1906.  
15073325 R.H.Baxter, N.Ponomarenko, V.Srajer, R.Pahl, K.Moffat, and J.R.Norris (2004).
Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center.
  Proc Natl Acad Sci U S A, 101, 5982-5987.
PDB code: 1r2c
15213381 R.Kort, H.Komori, S.Adachi, K.Miki, and A.Eker (2004).
DNA apophotolyase from Anacystis nidulans: 1.8 A structure, 8-HDF reconstitution and X-ray-induced FAD reduction.
  Acta Crystallogr D Biol Crystallogr, 60, 1205-1213.
PDB codes: 1owl 1owm 1own 1owo 1owp
15572444 S.Vaitheeswaran, H.Yin, J.C.Rasaiah, and G.Hummer (2004).
Water clusters in nonpolar cavities.
  Proc Natl Acad Sci U S A, 101, 17002-17005.  
15485258 S.Vaitheeswaran, J.C.Rasaiah, and G.Hummer (2004).
Electric field and temperature effects on water in the narrow nonpolar pores of carbon nanotubes.
  J Chem Phys, 121, 7955-7965.  
15341736 V.Adam, A.Royant, V.Nivière, F.P.Molina-Heredia, and D.Bourgeois (2004).
Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction.
  Structure, 12, 1729-1740.
PDB codes: 1vzg 1vzh 1vzi
12831319 D.F.Lewis (2003).
P450 structures and oxidative metabolism of xenobiotics.
  Pharmacogenomics, 4, 387-395.  
12950252 G.A.Schoch, R.Attias, M.Le Ret, and D.Werck-Reichhart (2003).
Key substrate recognition residues in the active site of a plant cytochrome P450, CYP73A1. Homology guided site-directed mutagenesis.
  Eur J Biochem, 270, 3684-3695.  
14529269 H.Zhang, L.Gruenke, D.Arscott, A.Shen, C.Kasper, D.L.Harris, M.Glavanovich, R.Johnson, and L.Waskell (2003).
Determination of the rate of reduction of oxyferrous cytochrome P450 2B4 by 5-deazariboflavin adenine dinucleotide T491V cytochrome P450 reductase.
  Biochemistry, 42, 11594-11603.  
12655052 J.A.Sigman, H.K.Kim, X.Zhao, J.R.Carey, and Y.Lu (2003).
The role of copper and protons in heme-copper oxidases: kinetic study of an engineered heme-copper center in myoglobin.
  Proc Natl Acad Sci U S A, 100, 3629-3634.  
12644707 M.H.Lim, J.U.Rohde, A.Stubna, M.R.Bukowski, M.Costas, R.Y.Ho, E.Munck, W.Nam, and L.Que (2003).
An FeIV=O complex of a tetradentate tripodal nonheme ligand.
  Proc Natl Acad Sci U S A, 100, 3665-3670.  
14502710 M.P.Jensen, M.P.Mehn, and L.Que (2003).
Intramolecular aromatic amination through iron-mediated nitrene transfer.
  Angew Chem Int Ed Engl, 42, 4357-4360.  
14556625 M.Strickler, B.M.Goldstein, K.Maxfield, L.Shireman, G.Kim, D.S.Matteson, and J.P.Jones (2003).
Crystallographic studies on the complex behavior of nicotine binding to P450cam (CYP101).
  Biochemistry, 42, 11943-11950.
PDB codes: 1p2y 1p7r
12668455 R.Fedorov, I.Schlichting, E.Hartmann, T.Domratcheva, M.Fuhrmann, and P.Hegemann (2003).
Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii.
  Biophys J, 84, 2474-2482.
PDB codes: 1n9l 1n9n 1n9o
14581231 S.Marchal, H.M.Girvan, A.C.Gorren, B.Mayer, A.W.Munro, C.Balny, and R.Lange (2003).
Formation of transient oxygen complexes of cytochrome p450 BM3 and nitric oxide synthase under high pressure.
  Biophys J, 85, 3303-3309.  
12771375 V.Guallar, M.H.Baik, S.J.Lippard, and R.A.Friesner (2003).
Peripheral heme substituents control the hydrogen-atom abstraction chemistry in cytochromes P450.
  Proc Natl Acad Sci U S A, 100, 6998-7002.  
12076537 A.W.Munro, D.G.Leys, K.J.McLean, K.R.Marshall, T.W.Ost, S.Daff, C.S.Miles, S.K.Chapman, D.A.Lysek, C.C.Moser, C.C.Page, and P.L.Dutton (2002).
P450 BM3: the very model of a modern flavocytochrome.
  Trends Biochem Sci, 27, 250-257.  
11916870 C.Tetreau, E.Novikov, M.Tourbez, and D.Lavalette (2002).
Kinetic evidence for three photolyzable taxonomic conformational substates in oxymyoglobin.
  Biophys J, 82, 2148-2155.  
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.  
12452431 F.P.Guengerich (2002).
Rate-limiting steps in cytochrome P450 catalysis.
  Biol Chem, 383, 1553-1564.  
15618693 H.Yasui, K.Deo, Y.Ogura, H.Yoshida, T.Shiraga, A.Kagayama, and H.Sakurai (2002).
Evidence for singlet oxygen involvement in rat and human cytochrome P450-dependent substrate oxidations.
  Drug Metab Pharmacokinet, 17, 416-426.  
11980473 J.P.Schelvis, V.Berka, G.T.Babcock, and A.L.Tsai (2002).
Resonance Raman detection of the Fe-S bond in endothelial nitric oxide synthase.
  Biochemistry, 41, 5695-5701.  
12134140 M.Kim, T.Okajima, S.Kishishita, M.Yoshimura, A.Kawamori, K.Tanizawa, and H.Yamaguchi (2002).
X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase.
  Nat Struct Biol, 9, 591-596.
PDB codes: 1ivu 1ivv 1ivw 1ivx
15618664 N.Murayama, T.Nakamura, M.Saeki, A.Soyama, Y.Saito, K.Sai, S.Ishida, O.Nakajima, M.Itoda, Y.Ohno, S.Ozawa, and J.Sawada (2002).
CYP3A4 gene polymorphisms influence testosterone 6beta-hydroxylation.
  Drug Metab Pharmacokinet, 17, 150-156.  
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.  
11976110 S.I.de Azevedo Wäsch, J.R.van der Ploeg, T.Maire, A.Lebreton, A.Kiener, and T.Leisinger (2002).
Transformation of isopropylamine to L-alaninol by Pseudomonas sp. strain KIE171 involves N-glutamylated intermediates.
  Appl Environ Microbiol, 68, 2368-2375.  
11914484 T.Ursby, M.Weik, E.Fioravanti, M.Delarue, M.Goeldner, and D.Bourgeois (2002).
Cryophotolysis of caged compounds: a technique for trapping intermediate states in protein crystals.
  Acta Crystallogr D Biol Crystallogr, 58, 607-614.
PDB codes: 1gsi 1gtv
  12039010 V.Guallar, B.F.Gherman, S.J.Lippard, and R.A.Friesner (2002).
Quantum chemical studies of methane monooxygenase: comparision with P450.
  Curr Opin Chem Biol, 6, 236-242.  
11981891 W.Nam, I.Kim, M.H.Lim, H.J.Choi, J.S.Lee, and H.G.Jang (2002).
Isolation of an oxomanganese(V) porphyrin intermediate in the reaction of a manganese(III) porphyrin complex and H2O2 in aqueous solution.
  Chemistry, 8, 2067-2071.  
  12039006 Y.Watanabe (2002).
Construction of heme enzymes: four approaches.
  Curr Opin Chem Biol, 6, 208-216.  
11121105 A.Celik, P.M.Cullis, M.J.Sutcliffe, R.Sangar, and E.L.Raven (2001).
Engineering the active site of ascorbate peroxidase.
  Eur J Biochem, 268, 78-85.  
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
  11738185 D.L.Harris (2001).
High-valent intermediates of heme proteins and model compounds.
  Curr Opin Chem Biol, 5, 724-735.  
11500894 F.Ogliaro, S.P.de Visser, J.T.Groves, and S.Shaik (2001).
Chameleon States: High-Valent Metal-Oxo Species of Cytochrome P450 and Its Ruthenium Analogue The research in HU was sponsored by the Binational German Israeli Foundation (GIF) and by the Israeli Ministry of Science, Culture and Sport. Partial support by the US National Science Foundation (CHE-9814301) to J.T.G. is acknowledged. F.O. thanks the EU for a Marie Curie Fellowship.
  Angew Chem Int Ed Engl, 40, 2874-2878.  
11331003 H.Li, C.S.Raman, P.Martásek, B.S.Masters, and T.L.Poulos (2001).
Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors.
  Biochemistry, 40, 5399-5406.
PDB codes: 1ed6 1foi 1fol 1foo 1fop
  11755401 J.M.Ogle, I.J.Clifton, P.J.Rutledge, J.M.Elkins, N.I.Burzlaff, R.M.Adlington, P.L.Roach, and J.E.Baldwin (2001).
Alternative oxidation by isopenicillin N synthase observed by X-ray diffraction.
  Chem Biol, 8, 1231-1237.
PDB codes: 1hb1 1hb2 1hb3 1hb4
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.  
11258940 Q.Xu, and M.R.Gunner (2001).
Trapping conformational intermediate states in the reaction center protein from photosynthetic bacteria.
  Biochemistry, 40, 3232-3241.  
11500893 S.P.de Visser, F.Ogliaro, and S.Shaik (2001).
How Does Ethene Inactivate Cytochrome P450 En Route to Its Epoxidation? A Density Functional Study The research is supported in part by the ISF and in part by the Ministry of Science, Culture, and Sport. F.O. acknowledges the European Union for a Marie Curie Fellowship.
  Angew Chem Int Ed Engl, 40, 2871-2874.  
  11578928 T.D.Bugg (2001).
Oxygenases: mechanisms and structural motifs for O(2) activation.
  Curr Opin Chem Biol, 5, 550-555.  
11389599 T.Sjodin, J.F.Christian, I.D.Macdonald, R.Davydov, M.Unno, S.G.Sligar, B.M.Hoffman, and P.M.Champion (2001).
Resonance Raman and EPR investigations of the D251N oxycytochrome P450cam/putidaredoxin complex.
  Biochemistry, 40, 6852-6859.  
11705368 Z.Ren, B.Perman, V.Srajer, T.Y.Teng, C.Pradervand, D.Bourgeois, F.Schotte, T.Ursby, R.Kort, M.Wulff, and K.Moffat (2001).
A molecular movie at 1.8 A resolution displays the photocycle of photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds.
  Biochemistry, 40, 13788-13801.  
  10975456 A.W.Munro, P.Taylor, and M.D.Walkinshaw (2000).
Structures of redox enzymes.
  Curr Opin Biotechnol, 11, 369-376.  
11114067 C.Jung (2000).
Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy.
  J Mol Recognit, 13, 325-351.  
11087371 C.Tetreau, M.Tourbez, and D.Lavalette (2000).
Conformational relaxation in hemoproteins: the cytochrome P-450cam case.
  Biochemistry, 39, 14219-14231.  
  11178272 D.Werck-Reichhart, and R.Feyereisen (2000).
Cytochromes P450: a success story.
  Genome Biol, 1, REVIEWS3003.  
  11102789 F.van Rantwijk, and R.A.Sheldon (2000).
Selective oxygen transfer catalysed by heme peroxidases: synthetic and mechanistic aspects.
  Curr Opin Biotechnol, 11, 554-564.  
11114513 I.Schlichting, and K.Chu (2000).
Trapping intermediates in the crystal: ligand binding to myoglobin.
  Curr Opin Struct Biol, 10, 744-752.  
  10975452 M.Olsen, B.Iverson, and G.Georgiou (2000).
High-throughput screening of enzyme libraries.
  Curr Opin Biotechnol, 11, 331-337.  
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.