spacer
spacer

PDBsum entry 1dcc

Go to PDB code: 
Top Page protein ligands links
Oxidoreductase(h2o2(a)) PDB id
1dcc
Contents
Protein chain
291 a.a.
Ligands
OXY-HEM
Waters ×182

References listed in PDB file
Key reference
Title 2.2 a structure of oxy-Peroxidase as a model for the transient enzyme: peroxide complex.
Authors M.A.Miller, A.Shaw, J.Kraut.
Ref. Nat Struct Biol, 1994, 1, 524-531.
PubMed id 7664080
Abstract
The Fe+3-OOH complex of peroxidases has a very short half life, and its structure cannot be determined by conventional methods. The Fe+2-O2 complex provides a useful structural model for this intermediate, as it differs by only one electron and one proton from the transient Fe+3-OOH complex. We therefore determined the crystal structure of the Fe+2-O2 complex formed by a yeast cytochrome c peroxidase mutant with Trp 191 replaced by Phe. The refined structure shows that dioxygen can form a hydrogen bond with the conserved distal His residue, but not with the conserved distal Arg residue. When the transient Fe+3-OOH complex is modelled in a similar orientation, the active site of peroxidase appears to be optimized for catalysing proton transfer between the vicinal oxygen atoms of the peroxy-anion.
Secondary reference #1
Title Reaction of ferrous cytochrome c peroxidase with dioxygen: site-Directed mutagenesis provides evidence for rapid reduction of dioxygen by intramolecular electron transfer from the compound i radical site.
Authors M.A.Miller, D.Bandyopadhyay, J.M.Mauro, T.G.Traylor, J.Kraut.
Ref. Biochemistry, 1992, 31, 2789-2797. [DOI no: 10.1021/bi00125a020]
PubMed id 1312347
Full text Abstract
Secondary reference #2
Title X-Ray structures of recombinant yeast cytochrome c peroxidase and three heme-Cleft mutants prepared by site-Directed mutagenesis.
Authors J.M.Wang, M.Mauro, S.L.Edwards, S.J.Oatley, L.A.Fishel, V.A.Ashford, N.H.Xuong, J.Kraut.
Ref. Biochemistry, 1990, 29, 7160-7173. [DOI no: 10.1021/bi00483a003]
PubMed id 2169873
Full text Abstract
Secondary reference #3
Title Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution.
Authors B.C.Finzel, T.L.Poulos, J.Kraut.
Ref. J Biol Chem, 1984, 259, 13027-13036.
PubMed id 6092361
Abstract
PROCHECK
Go to PROCHECK summary
 Headers

 

spacer

spacer