PDBsum entry 1kok

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Oxidoreductase PDB id
Protein chain
294 a.a. *
Waters ×620
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Crystal structure of mesopone cytochromE C peroxidase (mpccp)
Structure: CytochromE C peroxidase. Chain: a. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: opbyc. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
1.70Å     R-factor:   0.186     R-free:   0.207
Authors: B.Bhaskar,C.E.Immoos,M.S.Cohen,T.P.Barrows,P.J.Farmer, T.L.Poulos
Key ref: C.E.Immoos et al. (2002). Mesopone cytochrome c peroxidase: functional model of heme oxygenated oxidases. J Inorg Biochem, 91, 635-643. PubMed id: 12237229 DOI: 10.1016/S0162-0134(02)00447-6
20-Dec-01     Release date:   02-Oct-02    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P00431  (CCPR_YEAST) -  Cytochrome c peroxidase, mitochondrial
361 a.a.
294 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Cytochrome-c peroxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 ferrocytochrome c + H2O2 = 2 ferricytochrome c + 2 H2O
2 × ferrocytochrome c
+ H(2)O(2)
= 2 × ferricytochrome c
+ 2 × H(2)O
      Cofactor: Heme
Bound ligand (Het Group name = HIF) matches with 85.00% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     peroxidase activity     2 terms  


DOI no: 10.1016/S0162-0134(02)00447-6 J Inorg Biochem 91:635-643 (2002)
PubMed id: 12237229  
Mesopone cytochrome c peroxidase: functional model of heme oxygenated oxidases.
C.E.Immoos, B.Bhaskar, M.S.Cohen, T.P.Barrows, P.J.Farmer, T.L.Poulos.
The effect of heme ring oxygenation on enzyme structure and function has been examined in a reconstituted cytochrome c peroxidase. Oxochlorin derivatives were formed by OsO(4) treatment of mesoporphyrin followed by acid-catalyzed pinacol rearrangement. The northern oxochlorin isomers were isolated by chromatography, and the regio-isomers assignments determined by 2D COSY and NOE 1H NMR. The major isomer, 4-mesoporphyrinone (Mp), was metallated with FeCl(2) and reconstituted into cytochrome c peroxidase (CcP) forming a hybrid green protein, MpCcP. The heme-altered enzyme has 99% wild-type peroxidase activity with cytochrome c. EPR spectroscopy of MpCcP intermediate compound I verifies the formation of the Trp(191) radical similar to wild-type CcP in the reaction cycle. Peroxidase activity with small molecules is varied: guaiacol turnover increases approximately five-fold while that with ferrocyanide is approximately 85% of native. The electron-withdrawing oxo-substitutents on the cofactor cause a approximately 60-mV increase in Fe(III)/Fe(II) reduction potential. The present investigation represents the first structural characterization of an oxochlorin protein with X-ray intensity data collected to 1.70 A. Although a mixture of R- and S-mesopone isomers of the FeMP cofactor was used during heme incorporation into the apo-protein, only the S-isomer is found in the crystallized protein.

Literature references that cite this PDB file's key reference

  PubMed id Reference
15900441 B.Bhaskar, and T.L.Poulos (2005).
The 1.13-A structure of iron-free cytochrome c peroxidase.
  J Biol Inorg Chem, 10, 425-430.
PDB code: 1z53
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