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PDBsum entry 2cep

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Oxidoreductase(h2o2(a)) PDB id
2cep
Jmol
Contents
Protein chain
293 a.a. *
Ligands
HEM
Waters ×225
* Residue conservation analysis
PDB id:
2cep
Name: Oxidoreductase(h2o2(a))
Title: Role of met-230 in intramolecular electron transfer between the oxyferryl heme and trp 191 in cytochromE C peroxidase compound ii
Structure: CytochromE C peroxidase. Chain: a. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932
Resolution:
2.20Å     R-factor:   0.167    
Authors: G.W.Han,M.A.Miller,J.Kraut
Key ref:
R.Q.Liu et al. (1994). Role of methionine 230 in intramolecular electron transfer between the oxyferryl heme and tryptophan 191 in cytochrome c peroxidase compound II. Biochemistry, 33, 8678-8685. PubMed id: 8038157 DOI: 10.1021/bi00195a008
Date:
31-May-94     Release date:   31-Aug-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00431  (CCPR_YEAST) -  Cytochrome c peroxidase, mitochondrial
Seq:
Struc:
361 a.a.
293 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.1.11.1.5  - 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
Heme
Bound ligand (Het Group name = HEM) matches with 95.00% 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  

 

 
    reference    
 
 
DOI no: 10.1021/bi00195a008 Biochemistry 33:8678-8685 (1994)
PubMed id: 8038157  
 
 
Role of methionine 230 in intramolecular electron transfer between the oxyferryl heme and tryptophan 191 in cytochrome c peroxidase compound II.
R.Q.Liu, M.A.Miller, G.W.Han, S.Hahm, L.Geren, S.Hibdon, J.Kraut, B.Durham, F.Millett.
 
  ABSTRACT  
 
The kinetics of electron transfer from cytochrome c (CC) to yeast cytochrome c peroxidase (CcP) compound I were studied by flash photolysis and stopped-flow spectroscopy. Flash photolysis studies employed horse CC derivatives labeled at specific lysine amino groups with (dicarboxybipyridine)bis-(bipyridine)ruthenium (Ru-CC). Initial electron transfer from Ru-CC reduced the indole radical on Trp-191 of CcP compound I [CMPI(IV,R.)], producing CMPII(IV,R). This reaction was biphasic for each of several Ru-CC derivatives, with rate constants which varied according to the position of the Ru label. For Ru-27-CC labeled at lysine 27, rate constants of 43,000 and 1600 s-1 were observed at pH 5.0 in 2 mM acetate. After reduction of the indole radical by Ru-CC, intramolecular electron transfer from Trp-191 to the oxyferryl heme in CMPII(IV,R) was observed, producing CMPII(III,R.). The rate constant and extent of this intramolecular electron transfer reaction were independent of both the protein concentration and the Ru-CC derivative employed. The rate constant decreased from 1100 s-1 at pH 5 to 550 s-1 at pH 6, while the extent of conversion of CMPII(IV,R) to CMPII(III,R.) decreased from 56% at pH 5 to 29% at pH 6. The reaction was not detected at pH 7.0 and above. The pH dependence of the rate and extent of this internal electron transfer reaction paralleled the pH dependence of the rate of bimolecular reduction of CMPII(IV,R) by native horse CC measured by stopped-flow spectroscopy at high ionic strength.(ABSTRACT TRUNCATED AT 250 WORDS)
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
11900539 H.Mei, L.Geren, M.A.Miller, B.Durham, and F.Millett (2002).
Role of the low-affinity binding site in electron transfer from cytochrome C to cytochrome C peroxidase.
  Biochemistry, 41, 3968-3976.  
10346906 H.Mei, K.Wang, N.Peffer, G.Weatherly, D.S.Cohen, M.Miller, G.Pielak, B.Durham, and F.Millett (1999).
Role of configurational gating in intracomplex electron transfer from cytochrome c to the radical cation in cytochrome c peroxidase.
  Biochemistry, 38, 6846-6854.  
9485329 D.Sheng, and M.H.Gold (1998).
Irreversible oxidation of ferricytochrome c by lignin peroxidase.
  Biochemistry, 37, 2029-2036.  
9048579 E.Monzani, A.L.Gatti, A.Profumo, L.Casella, and M.Gullotti (1997).
Oxidation of phenolic compounds by lactoperoxidase. Evidence for the presence of a low-potential compound II during catalytic turnover.
  Biochemistry, 36, 1918-1926.  
8634253 C.A.Bonagura, M.Sundaramoorthy, H.S.Pappa, W.R.Patterson, and T.L.Poulos (1996).
An engineered cation site in cytochrome c peroxidase alters the reactivity of the redox active tryptophan.
  Biochemistry, 35, 6107-6115.  
8961943 H.Mei, K.Wang, S.McKee, X.Wang, J.L.Waldner, G.J.Pielak, B.Durham, and F.Millett (1996).
Control of formation and dissociation of the high-affinity complex between cytochrome c and cytochrome c peroxidase by ionic strength and the low-affinity binding site.
  Biochemistry, 35, 15800-15806.  
8823156 J.E.Morgan, M.I.Verkhovsky, and M.Wikström (1996).
Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase.
  Biochemistry, 35, 12235-12240.  
8942678 K.Wang, H.Mei, L.Geren, M.A.Miller, A.Saunders, X.Wang, J.L.Waldner, G.J.Pielak, B.Durham, and F.Millett (1996).
Design of a ruthenium-cytochrome c derivative to measure electron transfer to the radical cation and oxyferryl heme in cytochrome c peroxidase.
  Biochemistry, 35, 15107-15119.  
8547245 M.A.Miller, L.Geren, G.W.Han, A.Saunders, J.Beasley, G.J.Pielak, B.Durham, F.Millett, and J.Kraut (1996).
Identifying the physiological electron transfer site of cytochrome c peroxidase by structure-based engineering.
  Biochemistry, 35, 667-673.
PDB code: 1cyf
8961942 M.A.Miller (1996).
A complete mechanism for steady-state oxidation of yeast cytochrome c by yeast cytochrome c peroxidase.
  Biochemistry, 35, 15791-15799.  
8664277 S.K.Wilcox, G.M.Jensen, M.M.Fitzgerald, D.E.McRee, and D.B.Goodin (1996).
Altering substrate specificity at the heme edge of cytochrome c peroxidase.
  Biochemistry, 35, 4858-4866.
PDB codes: 3ccx 4ccx
8847347 F.Millett, M.A.Miller, L.Geren, and B.Durham (1995).
Electron transfer between cytochrome c and cytochrome c peroxidase.
  J Bioenerg Biomembr, 27, 341-351.  
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.