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PDBsum entry 2fe6
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protein ligands metals links
Oxidoreductase PDB id
2fe6

 

 

 

 

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Contents
Protein chain
405 a.a. *
Ligands
MNR
Metals
__K
Waters ×430
* Residue conservation analysis
PDB id:
2fe6
Name: Oxidoreductase
Title: P450cam from pseudomonas putida reconstituted with manganic protoporphyrin ix
Structure: Cytochrome p450-cam. Chain: a. Synonym: camphor 5-monooxygenase, p450cam. Engineered: yes
Source: Pseudomonas putida. Organism_taxid: 303. Gene: camc, cyp101. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.50Å     R-factor:   0.227     R-free:   0.249
Authors: K.Von Koenig,T.M.Makris,S.G.Sligar,I.Schlichting
Key ref: T.M.Makris et al. (2006). The status of high-valent metal oxo complexes in the P450 cytochromes. J Inorg Biochem, 100, 507-518. PubMed id: 16510191 DOI: 10.1016/j.jinorgbio.2006.01.025
Date:
15-Dec-05     Release date:   14-Mar-06    
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: 10.1016/j.jinorgbio.2006.01.025 J Inorg Biochem 100:507-518 (2006)
PubMed id: 16510191  
 
 
The status of high-valent metal oxo complexes in the P450 cytochromes.
T.M.Makris, K.von Koenig, I.Schlichting, S.G.Sligar.
 
  ABSTRACT  
 
The oxidative prowess of the P450 cytochromes in physiological reactions is attributed to the production of a high-valent iron-oxo complex, or Compound I intermediate, in the reaction cycle. Despite many years of study, however, the full electronic description of this fleeting intermediate still remains an active area of study. In this manuscript, the current status of the isolation and characterization of the P450 oxo-Fe(IV) is examined and compared to analogous states in related heme enzymes. In addition, the utilization of cofactor exchange to stabilize high-valent oxo-states in the P450 is addressed. Structural and spectroscopic studies on manganese reconstituted P450, and its corresponding oxo-complex, are presented.
 

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.  
21404414 T.Ying, F.Zhong, Z.H.Wang, W.Li, X.Tan, and Z.X.Huang (2011).
A route to novel functional metalloproteins via hybrids of cytochrome P450 and cytochrome c.
  Chembiochem, 12, 707-710.  
21071661 J.Rittle, and M.T.Green (2010).
Cytochrome P450 compound I: capture, characterization, and C-H bond activation kinetics.
  Science, 330, 933-937.  
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.  
20713732 T.M.Makris, M.Chakrabarti, E.Münck, and J.D.Lipscomb (2010).
A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis.
  Proc Natl Acad Sci U S A, 107, 15391-15396.  
19805032 A.Lewis-Ballester, D.Batabyal, T.Egawa, C.Lu, Y.Lin, M.A.Marti, L.Capece, D.A.Estrin, and S.R.Yeh (2009).
Evidence for a ferryl intermediate in a heme-based dioxygenase.
  Proc Natl Acad Sci U S A, 106, 17371-17376.  
19747698 A.R.Brash (2009).
Mechanistic aspects of CYP74 allene oxide synthases and related cytochrome P450 enzymes.
  Phytochemistry, 70, 1522-1531.  
19187034 H.C.Yeh, G.J.Gerfen, J.S.Wang, A.L.Tsai, and L.H.Wang (2009).
Characterization of the peroxidase mechanism upon reaction of prostacyclin synthase with peracetic acid. Identification of a tyrosyl radical intermediate.
  Biochemistry, 48, 917-928.  
19322428 J.Y.Lee, Y.M.Lee, H.Kotani, W.Nam, and S.Fukuzumi (2009).
High-valent manganese(v)-oxo porphyrin complexes in hydride transfer reactions.
  Chem Commun (Camb), (), 704-706.  
19572732 Q.Wang, X.Sheng, J.H.Horner, and M.Newcomb (2009).
Quantitative production of compound I from a cytochrome P450 enzyme at low temperatures. Kinetics, activation parameters, and kinetic isotope effects for oxidation of benzyl alcohol.
  J Am Chem Soc, 131, 10629-10636.  
18292895 A.R.Han, Y.Jin Jeong, Y.Kang, J.Y.Lee, M.Sook Seo, and W.Nam (2008).
Direct evidence for an iron(IV)-oxo porphyrin pi-cation radical as an active oxidant in catalytic oxygenation reactions.
  Chem Commun (Camb), (), 1076-1078.  
18196297 H.Hirao, K.B.Cho, and S.Shaik (2008).
QM/MM theoretical study of the pentacoordinate Mn(III) and resting states of manganese-reconstituted cytochrome P450(cam).
  J Biol Inorg Chem, 13, 521-530.  
18815130 J.Tejero, A.Biswas, Z.Q.Wang, R.C.Page, M.M.Haque, C.Hemann, J.L.Zweier, S.Misra, and D.J.Stuehr (2008).
Stabilization and Characterization of a Heme-Oxy Reaction Intermediate in Inducible Nitric-oxide Synthase.
  J Biol Chem, 283, 33498-33507.
PDB code: 3dwj
18278877 R.Zhang, and M.Newcomb (2008).
Laser flash photolysis generation of high-valent transition metal-oxo species: insights from kinetic studies in real time.
  Acc Chem Res, 41, 468-477.  
18788736 X.Sheng, J.H.Horner, and M.Newcomb (2008).
Spectra and kinetic studies of the compound I derivative of cytochrome P450 119.
  J Am Chem Soc, 130, 13310-13320.  
17893816 G.Lente, and I.Fábián (2007).
Kinetics and mechanism of the oxidation of water soluble porphyrin FeIIITPPS with hydrogen peroxide and the peroxomonosulfate ion.
  Dalton Trans, (), 4268-4275.  
17459323 H.C.Yeh, A.L.Tsai, and L.H.Wang (2007).
Reaction mechanisms of 15-hydroperoxyeicosatetraenoic acid catalyzed by human prostacyclin and thromboxane synthases.
  Arch Biochem Biophys, 461, 159-168.  
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.  
17630728 Z.Pan, and M.Newcomb (2007).
Kinetics and mechanism of oxidation reactions of porphyrin-iron(IV)-oxo intermediates.
  Inorg Chem, 46, 6767-6774.  
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 code is shown on the right.

 

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