Crystal structure of lignin peroxidase

Journal Article · Fri Jan 15 04:00:00 EST 1993 · Proceedings of the National Academy of Sciences of the United States of America; (United States)

DOI:https://doi.org/10.1073/pnas.90.2.750· OSTI ID:6389258

Edwards, S L ^[1]; Raag, R ^[2]; Wariishi, Hiroyuki; Gold, M H ^[3]; Poulos, T L ^[4]

---

1. Center for Advanced Research in Biotechnology, Rockville, MD (United States) National Institutes of Health, Bethesda, MD (United States)
2. Center for Advanced Research in Biotechnology, Rockville, MD (United States)
3. Oregon Graduate Institute of Science and Technology, Beaverton (United States)
4. Center for Advanced Reseaarch in Biotechnology, Rockville, MD (United States) Univ. of California, Irvine (United States)

The crystal structure of lignin peroxidase (LiP) from the basidiomycete Phanerochaete chrysosporium has been determined to 2.6 [Angstrom] resolution by using multiple isomorphous replacement methods and simulated annealing refinement. Of the 343 residues, residues 3-335 have been accounted for in the electron density map, including four disulfide bonds. The overall three-dimensional structure is very similar to the only other peroxidase in this group for which a high-resolution crystal structure is available, cytochrome c peroxidase, despite the fact that the sequence identity is only [approx]20%, LiP has four disulfide bonds, while cytochrome c peroxidase has none, and Lip is larger (343 vs. 294 residues). The basic helical fold and connectivity defined by 11 helical segments with the heme sandwiched between the distal and proximal helices found in cytochrome c peroxidase is maintained in LiP. Both enzymes have a histidine as a proximal heme ligand, which is hydrogen bonded to a buried aspartic acid side chain. The distal or peroxide binding pocket also is similar, including the distal arginine and histidine. The most striking difference is that, whereas cytochrome c peroxidase has tryptophans contacting the distal and proximal heme surfaces, LiP has phenylalanines. This in part explains why, in the reaction with peroxides, cytochrome c peroxidase forms an amino acid-centered free radical, whereas LiP forms a porphyrin [pi] cation radical. 42 refs., 4 figs., 2 tabs.

• OSTI ID: 6389258
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (United States), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (United States) Vol. 90:2; ISSN PNASA6; ISSN 0027-8424
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
ARGININE
ASPARTIC ACID
AZOLES
CARBOHYDRATES
CARBOXYLIC ACIDS
CRYSTAL STRUCTURE
ELEMENTS
ENZYME ACTIVITY
ENZYMES
EUMYCOTA
FUNGI
HEME
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HISTIDINE
HYDROGEN
IMIDAZOLES
LIGNIN
NONMETALS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
OXYGEN COMPOUNDS
PEROXIDES
PHANEROCHAETE
PIGMENTS
PLANTS
POLYSACCHARIDES
PORPHYRINS
PROTEINS
SACCHARIDES