Redox equilibria of manganese peroxidase from Phanerochaetes chrysosporium: Functional role of residues on the proximal side of the haem pocket

Roberta Santucci, Cristiana Bongiovanni, Stefano Marini, Rebecca Del Conte, Ming Tien, Lucia Banci, Massimo Coletta

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Redox potentials of recombinant manganese peroxidase from Phanerochaeres chrysosporium have been measured by cyclic voltammetry as a function of pH, between pH 4.5 and pH 10.5. They display a bimodal behaviour (characterized by an 'alkaline' and an 'acid' transition), which indicates that (at least) two protonating groups change their pK(b) values upon reduction (and/or oxidation) of the iron atom in haem. Analogous measurements have been carried out on four site-directed mutants involving residues in close proximity to the proximal ligand, His173, in order to investigate the role played by residues of the proximal haem pocket on the redox properties of this enzyme. Results obtained suggest that the protonation state of N(δ) of the proximal imidazole group is redox-linked and that it is crucial in regulating the 'alkaline' transition. On the other hand, none of the proximal mutants alters the 'acid' transition, suggesting that it is modulated by groups located in a different portion of the protein.

Original languageEnglish (US)
Pages (from-to)85-90
Number of pages6
JournalBiochemical Journal
Volume349
Issue number1
DOIs
StatePublished - Jul 1 2000

Fingerprint

manganese peroxidase
Chrysosporium
Heme
Oxidation-Reduction
Acids
Protonation
Cyclic voltammetry
Iron
Ligands
Atoms
Oxidation
Enzymes
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Santucci, Roberta ; Bongiovanni, Cristiana ; Marini, Stefano ; Del Conte, Rebecca ; Tien, Ming ; Banci, Lucia ; Coletta, Massimo. / Redox equilibria of manganese peroxidase from Phanerochaetes chrysosporium : Functional role of residues on the proximal side of the haem pocket. In: Biochemical Journal. 2000 ; Vol. 349, No. 1. pp. 85-90.
@article{7415761aeec84a59b63147d3f608f281,
title = "Redox equilibria of manganese peroxidase from Phanerochaetes chrysosporium: Functional role of residues on the proximal side of the haem pocket",
abstract = "Redox potentials of recombinant manganese peroxidase from Phanerochaeres chrysosporium have been measured by cyclic voltammetry as a function of pH, between pH 4.5 and pH 10.5. They display a bimodal behaviour (characterized by an 'alkaline' and an 'acid' transition), which indicates that (at least) two protonating groups change their pK(b) values upon reduction (and/or oxidation) of the iron atom in haem. Analogous measurements have been carried out on four site-directed mutants involving residues in close proximity to the proximal ligand, His173, in order to investigate the role played by residues of the proximal haem pocket on the redox properties of this enzyme. Results obtained suggest that the protonation state of N(δ) of the proximal imidazole group is redox-linked and that it is crucial in regulating the 'alkaline' transition. On the other hand, none of the proximal mutants alters the 'acid' transition, suggesting that it is modulated by groups located in a different portion of the protein.",
author = "Roberta Santucci and Cristiana Bongiovanni and Stefano Marini and {Del Conte}, Rebecca and Ming Tien and Lucia Banci and Massimo Coletta",
year = "2000",
month = "7",
day = "1",
doi = "10.1042/0264-6021:3490085",
language = "English (US)",
volume = "349",
pages = "85--90",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "1",

}

Redox equilibria of manganese peroxidase from Phanerochaetes chrysosporium : Functional role of residues on the proximal side of the haem pocket. / Santucci, Roberta; Bongiovanni, Cristiana; Marini, Stefano; Del Conte, Rebecca; Tien, Ming; Banci, Lucia; Coletta, Massimo.

In: Biochemical Journal, Vol. 349, No. 1, 01.07.2000, p. 85-90.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Redox equilibria of manganese peroxidase from Phanerochaetes chrysosporium

T2 - Functional role of residues on the proximal side of the haem pocket

AU - Santucci, Roberta

AU - Bongiovanni, Cristiana

AU - Marini, Stefano

AU - Del Conte, Rebecca

AU - Tien, Ming

AU - Banci, Lucia

AU - Coletta, Massimo

PY - 2000/7/1

Y1 - 2000/7/1

N2 - Redox potentials of recombinant manganese peroxidase from Phanerochaeres chrysosporium have been measured by cyclic voltammetry as a function of pH, between pH 4.5 and pH 10.5. They display a bimodal behaviour (characterized by an 'alkaline' and an 'acid' transition), which indicates that (at least) two protonating groups change their pK(b) values upon reduction (and/or oxidation) of the iron atom in haem. Analogous measurements have been carried out on four site-directed mutants involving residues in close proximity to the proximal ligand, His173, in order to investigate the role played by residues of the proximal haem pocket on the redox properties of this enzyme. Results obtained suggest that the protonation state of N(δ) of the proximal imidazole group is redox-linked and that it is crucial in regulating the 'alkaline' transition. On the other hand, none of the proximal mutants alters the 'acid' transition, suggesting that it is modulated by groups located in a different portion of the protein.

AB - Redox potentials of recombinant manganese peroxidase from Phanerochaeres chrysosporium have been measured by cyclic voltammetry as a function of pH, between pH 4.5 and pH 10.5. They display a bimodal behaviour (characterized by an 'alkaline' and an 'acid' transition), which indicates that (at least) two protonating groups change their pK(b) values upon reduction (and/or oxidation) of the iron atom in haem. Analogous measurements have been carried out on four site-directed mutants involving residues in close proximity to the proximal ligand, His173, in order to investigate the role played by residues of the proximal haem pocket on the redox properties of this enzyme. Results obtained suggest that the protonation state of N(δ) of the proximal imidazole group is redox-linked and that it is crucial in regulating the 'alkaline' transition. On the other hand, none of the proximal mutants alters the 'acid' transition, suggesting that it is modulated by groups located in a different portion of the protein.

UR - http://www.scopus.com/inward/record.url?scp=0034235415&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034235415&partnerID=8YFLogxK

U2 - 10.1042/0264-6021:3490085

DO - 10.1042/0264-6021:3490085

M3 - Article

C2 - 10861214

AN - SCOPUS:0034235415

VL - 349

SP - 85

EP - 90

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 1

ER -