A comparative reactivity study of microperoxidases based on hemin, mesohemin and deuterohemin

Ekaterina S. Ryabova, Patrik Rydberg, Matthias Kolberg, Espen Harbitz, Anne Laure Barra, Ulf Ryde, K. Kristoffer Andersson, Ebbe Nordlander

Research output: Contribution to journalArticle

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Abstract

Three microperoxidases - hemin-6(7)-gly-gly-his methyl ester (HGGH), mesohemin-6(7)-gly-gly-his methyl ester (MGGH) and deuterohemin-6(7)-gly-gly-his methyl ester (DGGH) - have been prepared as models for heme-containing peroxidases by condensation of glycyl-glycyl-l-histidine methyl ester with the propionic side chains of hemin, mesohemin and deuterohemin, respectively. The three microperoxidases differ in two substituents, R, of the protoporphyrin IX framework (HGGH: R = vinyl, MGGH: R = ethyl, DGGH: R = H). X-band and high field EPR spectra show that the microperoxidases exhibit spectroscopic properties similar to those of metmyoglobin, i.e. a high spin ferric S = 5/2 signal at g = 6 and g = 2 and an estimated D value of 7.5 ± 1 cm-1. The catalytic activities of the microperoxidases towards K4[Fe(CN)6], l-tyrosine methyl ester and 2,2′-azino(bis(3-ethylbenzothiazoline-6-sulfonic acid)) (ABTS) have been investigated. It was found that all three microperoxidases exhibit peroxidase activity and that the reactions follow the generally accepted peroxidase reaction scheme [Biochem. J. 145 (1975) 93-103] with the exception that the initial formation of a Compound I analogue is the rate-limiting step for the whole process. The general activity trend was found to be MGGH ≈ DGGH > HGGH. For each microperoxidase, DFT calculations (B3LYP) were made on the reactions of compounds 0, I and II with H+, e- and H + + e-, respectively, in order to probe the possible relationship between the nature of the 2- and 4-substituents of the hemin and the observed reactivity. The computational modeling indicates that the relative energy differences are very small; solvation and electrostatic effects may be factors that decide the relative activities of the microperoxidases.

Original languageEnglish (US)
Pages (from-to)852-863
Number of pages12
JournalJournal of Inorganic Biochemistry
Volume99
Issue number3
DOIs
StatePublished - Mar 2005

Fingerprint

diglycyl-histidine
Hemin
Esters
Peroxidase
Metmyoglobin
Peroxidases
Sulfonic Acids
Solvation
Heme
Discrete Fourier transforms
Paramagnetic resonance
Condensation
Electrostatics
Catalyst activity
Static Electricity
deuterohemin

Keywords

  • Catalysis
  • Peptide
  • Peroxidase
  • Protopoporphyrin IX

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

A comparative reactivity study of microperoxidases based on hemin, mesohemin and deuterohemin. / Ryabova, Ekaterina S.; Rydberg, Patrik; Kolberg, Matthias; Harbitz, Espen; Barra, Anne Laure; Ryde, Ulf; Andersson, K. Kristoffer; Nordlander, Ebbe.

In: Journal of Inorganic Biochemistry, Vol. 99, No. 3, 03.2005, p. 852-863.

Research output: Contribution to journalArticle

Ryabova, ES, Rydberg, P, Kolberg, M, Harbitz, E, Barra, AL, Ryde, U, Andersson, KK & Nordlander, E 2005, 'A comparative reactivity study of microperoxidases based on hemin, mesohemin and deuterohemin', Journal of Inorganic Biochemistry, vol. 99, no. 3, pp. 852-863. https://doi.org/10.1016/j.jinorgbio.2004.12.020
Ryabova, Ekaterina S. ; Rydberg, Patrik ; Kolberg, Matthias ; Harbitz, Espen ; Barra, Anne Laure ; Ryde, Ulf ; Andersson, K. Kristoffer ; Nordlander, Ebbe. / A comparative reactivity study of microperoxidases based on hemin, mesohemin and deuterohemin. In: Journal of Inorganic Biochemistry. 2005 ; Vol. 99, No. 3. pp. 852-863.
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AU - Andersson, K. Kristoffer

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N2 - Three microperoxidases - hemin-6(7)-gly-gly-his methyl ester (HGGH), mesohemin-6(7)-gly-gly-his methyl ester (MGGH) and deuterohemin-6(7)-gly-gly-his methyl ester (DGGH) - have been prepared as models for heme-containing peroxidases by condensation of glycyl-glycyl-l-histidine methyl ester with the propionic side chains of hemin, mesohemin and deuterohemin, respectively. The three microperoxidases differ in two substituents, R, of the protoporphyrin IX framework (HGGH: R = vinyl, MGGH: R = ethyl, DGGH: R = H). X-band and high field EPR spectra show that the microperoxidases exhibit spectroscopic properties similar to those of metmyoglobin, i.e. a high spin ferric S = 5/2 signal at g⊥ = 6 and g∥ = 2 and an estimated D value of 7.5 ± 1 cm-1. The catalytic activities of the microperoxidases towards K4[Fe(CN)6], l-tyrosine methyl ester and 2,2′-azino(bis(3-ethylbenzothiazoline-6-sulfonic acid)) (ABTS) have been investigated. It was found that all three microperoxidases exhibit peroxidase activity and that the reactions follow the generally accepted peroxidase reaction scheme [Biochem. J. 145 (1975) 93-103] with the exception that the initial formation of a Compound I analogue is the rate-limiting step for the whole process. The general activity trend was found to be MGGH ≈ DGGH > HGGH. For each microperoxidase, DFT calculations (B3LYP) were made on the reactions of compounds 0, I and II with H+, e- and H + + e-, respectively, in order to probe the possible relationship between the nature of the 2- and 4-substituents of the hemin and the observed reactivity. The computational modeling indicates that the relative energy differences are very small; solvation and electrostatic effects may be factors that decide the relative activities of the microperoxidases.

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