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Article

Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase.

Proceedings of the National Academy of Sciences of the United States of America - 22 Sept 2009

Smith Andrew T, Doyle Wendy A, Dorlet Pierre, Ivancich Anabella

Abstract excerpt

The surface oxidation site (Trp-171) in lignin peroxidase (LiP) required for the reaction with veratryl alcohol a high-redox-potential (1.4 V) substrate, was engineered into Coprinus cinereus peroxidase (CiP) by introducing a Trp residue into a heme peroxidase that has similar protein fold but lacks this activity. To create the catalytic activity toward veratryl alcohol in CiP, it was necessary to reproduce the...

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Source

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Identifiers

PMID: 19805263
DOI: 10.1073/pnas.0904535106
PMCID: PMC2752603

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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