SGD DescriptionMitochondrial cytochrome-c peroxidase; degrades reactive oxygen species in mitochondria, involved in the response to oxidative stress
AspGD DescriptionCytochrome-c peroxidase precursor
References
Takio K, et al. (1980 Sep). Primary structure of yeast cytochrome c peroxidase. II. The complete amino acid sequence.
Kaput J, et al. (1982 Dec 25). Nucleotide sequence of the yeast nuclear gene for cytochrome c peroxidase precursor. Functional implications of the pre sequence for protein transport into mitochondria.
Goltz S, et al. (1982 Sep 25). Isolation of the yeast nuclear gene encoding the mitochondrial protein, cytochrome c peroxidase.
Finzel BC, et al. (1984 Nov 10). Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution.
Mauro JM, et al. (1988 Aug 23). Tryptophan-191----phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation.
Wang JM, et al. (1990 Aug 7). X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis.
Goodin DB, et al. (1993 Apr 6). The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme.
Fitzgerald MM, et al. (1996 Jul). A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity.
Hirst J, et al. (2000 Mar 24). Unusual oxidative chemistry of N(omega)-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase.
Hirst J, et al. (2001 Feb 6). Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 1. Effects on structure.
Sato I, et al. (2009 Mar 20). The glutathione system of Aspergillus nidulans involves a fungus-specific glutathione S-transferase.
Pusztahelyi T, et al. (2011 Feb). Comparison of transcriptional and translational changes caused by long-term menadione exposure in Aspergillus nidulans.