Electrostatic modulation of electron transfer in the active site of heme peroxidases

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

The heme enyzmes cytochrome c peroxidase (CCP) and pea cytosolic ascorbate peroxidase (APX) show a high level of sequence identity. The main difference near the active sites is the presence of a cation binding site in APX located about 1 nm from the Trp-179 side chain, which is hydrogen-bonded to Asp-208. It is possible that this difference in electrostatics provided by the protein environment is an essential determinant of the stabilization of the ion-pair or neutral form of the Trp...Asp couple in APX and CCP. Semiempirical molecular orbital calculations support the hypothesis that the position of the moving proton inside the couple influences the location of the free electron, leading to radical formation either on the heme or on the Trp side chain of these enzymes.

Original languageEnglish
Pages (from-to)135-138
Number of pages4
JournalJournal of Biological Inorganic Chemistry
Volume2
Issue number1
DOIs
Publication statusPublished - Feb 1997

Fingerprint

Ascorbate Peroxidases
Peroxidases
Static Electricity
Heme
Cytochrome-c Peroxidase
Electrostatics
Catalytic Domain
Modulation
Electrons
Orbital calculations
Peas
Molecular orbitals
Viperidae
Cations
Protons
Hydrogen
Stabilization
Binding Sites
Ions
Enzymes

Keywords

  • Free radical location
  • Heme peroxidases
  • Molecular orbital calculations
  • Protein electrostatics

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Electrostatic modulation of electron transfer in the active site of heme peroxidases. / Náray-Szabó, G.

In: Journal of Biological Inorganic Chemistry, Vol. 2, No. 1, 02.1997, p. 135-138.

Research output: Contribution to journalArticle

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