Proton NMR investigation into the basis for the relatively high redox potential of lignin peroxidase

Lucia Banci, Ivano Bertini, Paola Turano, Ming Tien, T. Kent Kirk

Research output: Contribution to journalArticle

97 Citations (Scopus)

Abstract

Lignin peroxidase shares several structural features with the well-studied horseradish peroxidase and cytochrome c peroxidase but carries a higher redox potential. Here the heme domain of lignin peroxidase and the lignin peroxidase cyanide adduct was examined by 1H NMR spectroscopy, including nuclear Overhauser effect and two-dimensional measurements, and the findings were compared with those for horseradish peroxidase and cytochrome c peroxidase. Structural information was obtained on the orientation of the heme vinyl and propionate groups and the proximal and distal histidines. The shifts of the el proton of the proximal histidine were found to be empirically related to the Fe3+/Fe2+ redox potentials.

Original languageEnglish (US)
Pages (from-to)6956-6960
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number16
DOIs
StatePublished - Jan 1 1991

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Cytochrome-c Peroxidase
Oxidation-Reduction
Protons
Horseradish Peroxidase
Heme
Histidine
Propionates
Cyanides
Magnetic Resonance Spectroscopy
lignin peroxidase

All Science Journal Classification (ASJC) codes

  • General

Cite this

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Proton NMR investigation into the basis for the relatively high redox potential of lignin peroxidase. / Banci, Lucia; Bertini, Ivano; Turano, Paola; Tien, Ming; Kirk, T. Kent.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, No. 16, 01.01.1991, p. 6956-6960.

Research output: Contribution to journalArticle

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T1 - Proton NMR investigation into the basis for the relatively high redox potential of lignin peroxidase

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AU - Bertini, Ivano

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AU - Kirk, T. Kent

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