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

Ryabova, Ekaterina LU ; Rydberg, Patrik LU ; Kolberg, M; Harbitz, E; Barra, A L; Ryde, Ulf LU ; Andersson, K K and Nordlander, Ebbe LU (2005) In Journal of Inorganic Biochemistry 99(3). p.852-863
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(perpendicular to) = 6 and g(parallel to) = 2 and an estimated... (More)
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(perpendicular to) = 6 and g(parallel to) = 2 and an estimated D value of 7.5 +/- 1 cm(-1). The catalytic activities of the microperoxidases towards K-4[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 approximate to 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. (C) 2005 Elsevier Inc. All rights reserved. (Less)
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author
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type
Contribution to journal
publication status
published
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in
Journal of Inorganic Biochemistry
volume
99
issue
3
pages
852 - 863
publisher
Elsevier
external identifiers
  • wos:000227374900021
  • pmid:15708807
  • scopus:13844271238
ISSN
1873-3344
DOI
10.1016/j.jinorgbio.2004.12.020
language
English
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yes
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55312bde-2659-480d-af90-659b5494afb4 (old id 152782)
date added to LUP
2007-07-09 14:10:07
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2017-07-02 04:31:02
@article{55312bde-2659-480d-af90-659b5494afb4,
  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(perpendicular to) = 6 and g(parallel to) = 2 and an estimated D value of 7.5 +/- 1 cm(-1). The catalytic activities of the microperoxidases towards K-4[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 approximate to 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. (C) 2005 Elsevier Inc. All rights reserved.},
  author       = {Ryabova, Ekaterina and Rydberg, Patrik and Kolberg, M and Harbitz, E and Barra, A L and Ryde, Ulf and Andersson, K K and Nordlander, Ebbe},
  issn         = {1873-3344},
  language     = {eng},
  number       = {3},
  pages        = {852--863},
  publisher    = {Elsevier},
  series       = {Journal of Inorganic Biochemistry},
  title        = {A comparative reactivity study of microperoxidases based on hemin, mesohemin and deuterohemin},
  url          = {http://dx.doi.org/10.1016/j.jinorgbio.2004.12.020},
  volume       = {99},
  year         = {2005},
}