1H NMR Investigation of Manganese Peroxidase from Phanerochaete chrysosporium. A Comparison with Other Peroxidases

Lucia Banci, Ivano Bertini, Paola Turano, Elizabeth A. Pease, Ming Tien

Research output: Contribution to journalArticle

67 Citations (Scopus)

Abstract

1H NMR spectra at 200-and 600-MHz of manganese peroxidase from Phanerochaete chrysosporium and of its cyanide derivative are reported. The spectrum of the native protein is very similar to that of other peroxidases. The assignment of the spectrum of the cyanide derivative has been performed through ID NOE, 2D NOESY, and COSY experiments. This protein is very similar to lignin peroxidase, the only meaningful difference being the shift of H52 of the proximal histidine. The spectra of the cyanide derivative of these two proteins are compared with those of horseradish peroxidase and cytochrome c peroxidase. The shift pattern of the protons of the proximal histidine is discussed relative to the structural properties which affect the Fe3+/Fe2+ redox potential.

Original languageEnglish (US)
Pages (from-to)10009-10017
Number of pages9
JournalBiochemistry
Volume31
Issue number41
DOIs
StatePublished - Feb 1 1992

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manganese peroxidase
Phanerochaete
Peroxidases
Cyanides
Nuclear magnetic resonance
Derivatives
Histidine
Cytochrome-c Peroxidase
Proteins
Horseradish Peroxidase
Oxidation-Reduction
Protons
Structural properties
Proton Magnetic Resonance Spectroscopy
Experiments

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Banci, Lucia ; Bertini, Ivano ; Turano, Paola ; Pease, Elizabeth A. ; Tien, Ming. / 1H NMR Investigation of Manganese Peroxidase from Phanerochaete chrysosporium. A Comparison with Other Peroxidases. In: Biochemistry. 1992 ; Vol. 31, No. 41. pp. 10009-10017.
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abstract = "1H NMR spectra at 200-and 600-MHz of manganese peroxidase from Phanerochaete chrysosporium and of its cyanide derivative are reported. The spectrum of the native protein is very similar to that of other peroxidases. The assignment of the spectrum of the cyanide derivative has been performed through ID NOE, 2D NOESY, and COSY experiments. This protein is very similar to lignin peroxidase, the only meaningful difference being the shift of H52 of the proximal histidine. The spectra of the cyanide derivative of these two proteins are compared with those of horseradish peroxidase and cytochrome c peroxidase. The shift pattern of the protons of the proximal histidine is discussed relative to the structural properties which affect the Fe3+/Fe2+ redox potential.",
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1H NMR Investigation of Manganese Peroxidase from Phanerochaete chrysosporium. A Comparison with Other Peroxidases. / Banci, Lucia; Bertini, Ivano; Turano, Paola; Pease, Elizabeth A.; Tien, Ming.

In: Biochemistry, Vol. 31, No. 41, 01.02.1992, p. 10009-10017.

Research output: Contribution to journalArticle

TY - JOUR

T1 - 1H NMR Investigation of Manganese Peroxidase from Phanerochaete chrysosporium. A Comparison with Other Peroxidases

AU - Banci, Lucia

AU - Bertini, Ivano

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AU - Pease, Elizabeth A.

AU - Tien, Ming

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AB - 1H NMR spectra at 200-and 600-MHz of manganese peroxidase from Phanerochaete chrysosporium and of its cyanide derivative are reported. The spectrum of the native protein is very similar to that of other peroxidases. The assignment of the spectrum of the cyanide derivative has been performed through ID NOE, 2D NOESY, and COSY experiments. This protein is very similar to lignin peroxidase, the only meaningful difference being the shift of H52 of the proximal histidine. The spectra of the cyanide derivative of these two proteins are compared with those of horseradish peroxidase and cytochrome c peroxidase. The shift pattern of the protons of the proximal histidine is discussed relative to the structural properties which affect the Fe3+/Fe2+ redox potential.

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