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PDBsum entry 1h7k

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Oxidoreductase PDB id
1h7k
Jmol
Contents
Protein chain
476 a.a. *
Ligands
HEM
ACT
SO4
Waters ×168
* Residue conservation analysis
PDB id:
1h7k
Name: Oxidoreductase
Title: Formation of a tyrosyl radical intermediate in proteus mirabilis catalase by directed mutagenesis and consequences for nucleotide reactivity
Structure: Catalase. Chain: a. Engineered: yes. Other_details: methionine sulfone in position 53, tyrosine 337 lack the hydroxyl hydrogen
Source: Proteus mirabilis. Expressed in: escherichia coli.
Biol. unit: Tetramer (from PDB file)
Resolution:
2.40Å     R-factor:   0.237     R-free:   0.240
Authors: P.Andreoletti,S.Gambarelli,J.Gaillard,G.Sainz,V.Stojanoff, H.M.Jouve
Key ref:
P.Andreoletti et al. (2001). Formation of a tyrosyl radical intermediate in Proteus mirabilis catalase by directed mutagenesis and consequences for nucleotide reactivity. Biochemistry, 40, 13734-13743. PubMed id: 11695923 DOI: 10.1021/bi010687f
Date:
08-Jul-01     Release date:   25-Feb-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P42321  (CATA_PROMI) -  Catalase
Seq:
Struc:
484 a.a.
476 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.1.11.1.6  - Catalase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 H2O2 = O2 + 2 H2O
2 × H(2)O(2)
= O(2)
+ 2 × H(2)O
      Cofactor: Heme; Mn(2+)
Heme
Bound ligand (Het Group name = HEM) matches with 95.00% similarity
Mn(2+)
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 process   3 terms 
  Biochemical function     oxidoreductase activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1021/bi010687f Biochemistry 40:13734-13743 (2001)
PubMed id: 11695923  
 
 
Formation of a tyrosyl radical intermediate in Proteus mirabilis catalase by directed mutagenesis and consequences for nucleotide reactivity.
P.Andreoletti, S.Gambarelli, G.Sainz, V.Stojanoff, C.White, G.Desfonds, J.Gagnon, J.Gaillard, H.M.Jouve.
 
  ABSTRACT  
 
Proteus mirabilis catalase (PMC) belongs to the family of NADPH binding catalases. The function of NADPH in these enzymes is still a matter of debate. This study presents the effects of two independent phenylalanine mutations (F194 and F215), located between NADPH and heme in the PMC structure. The phenylalanines were replaced with tyrosines which we predicted could carry radicals in a NADPH-heme electron transfer. The X-ray crystal structures of the two mutants indicated that neither the binding site of NADPH nor the immediate environment of the residues was affected by the mutations. Measurements using H2O2 as a substrate confirmed that the variants were as active as the native enzyme. With equivalent amounts of peroxoacetic acid, wild-type PMC, F215Y PMC, and beef liver catalase (BLC) formed a stable compound I, while the F194Y PMC variant produced a compound I which was rapidly transformed into compound II and a tyrosyl radical. EPR studies showed that this radical, generated by the oxidation of Y194, was not related to the previously observed radical in BLC, located on Y369. In the presence of excess NADPH, compound I was reduced to a resting enzyme (k(obs) = 1.7 min(-1)) in a two-electron process. This was independent of the enzyme's origin and did not require any thus far identified tyrosyl radicals. Conversely, the presence of a tyrosyl radical in F194Y PMC greatly enhanced the oxidation of reduced beta-nicotinamide mononucleotide under a steady-state H2O2 flow with observable compound II. This process could involve a one-electron reduction of compound I via Y194.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
17158050 H.N.Kirkman, and G.F.Gaetani (2007).
Mammalian catalase: a venerable enzyme with new mysteries.
  Trends Biochem Sci, 32, 44-50.  
17237942 O.Horner, J.M.Mouesca, P.L.Solari, M.Orio, J.L.Oddou, P.Bonville, and H.M.Jouve (2007).
Spectroscopic description of an unusual protonated ferryl species in the catalase from Proteus mirabilis and density functional theory calculations on related models. Consequences for the ferryl protonation state in catalase, peroxidase and chloroperoxidase.
  J Biol Inorg Chem, 12, 509-525.  
16298761 H.de Groot, O.Auferkamp, T.Bramey, K.de Groot, M.Kirsch, H.G.Korth, F.Petrat, and R.Sustmann (2006).
Non-oxygen-forming pathways of hydrogen peroxide degradation by bovine liver catalase at low hydrogen peroxide fluxes.
  Free Radic Res, 40, 67-74.  
16609813 M.S.Lorentzen, E.Moe, H.M.Jouve, and N.P.Willassen (2006).
Cold adapted features of Vibrio salmonicida catalase: characterisation and comparison to the mesophilic counterpart from Proteus mirabilis.
  Extremophiles, 10, 427-440.  
12779342 F.Wu, L.J.Katsir, M.Seavy, and B.J.Gaffney (2003).
Role of radical formation at tyrosine 193 in the allene oxide synthase domain of a lipoxygenase-AOS fusion protein from coral.
  Biochemistry, 42, 6871-6880.  
12486720 P.Andreoletti, G.Sainz, M.Jaquinod, J.Gagnon, and H.M.Jouve (2003).
High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron.
  Proteins, 50, 261-271.
PDB codes: 1e93 1h6n
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