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Article

Manganese oxidation site in Pleurotus eryngii versatile peroxidase: a site-directed mutagenesis, kinetic, and crystallographic study.

Biochemistry - 9 Jan 2007

Ruiz-Dueñas Francisco J, Morales María, Pérez-Boada Marta, Choinowski Thomas, Martínez María Jesús, Piontek Klaus, Martínez Angel T

Abstract excerpt

The molecular architecture of versatile peroxidase (VP) includes an exposed tryptophan responsible for aromatic substrate oxidation and a putative Mn2+ oxidation site. The crystal structures (solved up to 1.3 A) of wild-type and recombinant Pleurotus eryngii VP, before and after exposure to Mn2+, showed a variable orientation of the Glu36 and Glu40 side chains that, together with Asp175, contribute to Mn2+...

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PMID: 17198376
DOI: 10.1021/bi061542h

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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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