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Preparation and reactivity studies of synthetic microperoxidases containing b-type heme

Ryabova, Ekaterina LU ; Dikiy, Alexander; Hesslein, Ashley E; Bjerrum, Morten J; Ciurli, Stefano and Nordlander, Ebbe LU (2004) In Journal of Biological Inorganic Chemistry 9(4). p.385-395
Abstract
In order to create a heme environment that permits biomimicry of heme-containing peroxidases, a number of new hemin–peptide complexes—hemin-2(18)-glycyl-l-histidine methyl ester (HGH), hemin-2(18)-glycyl-glycyl-l-histidine methyl ester (HGGH), and hemin-2,18-bis(glycyl-glycyl-l-histidine methyl ester) (H2GGH)—have been prepared by condensation of glycyl-l-histidine methyl ester or glycyl-glycyl-l-histidine methyl ester with the propionic side chains of hemin. Characterization by means of UV/vis- and 1H NMR spectroscopy as well as cyclic- and differential pulse voltammetry indicates the formation of five-coordinate complexes in the case of HGH and HGGH, with histidine as an axial ligand. In the case of H2GGH, a six-coordinate complex with... (More)
In order to create a heme environment that permits biomimicry of heme-containing peroxidases, a number of new hemin–peptide complexes—hemin-2(18)-glycyl-l-histidine methyl ester (HGH), hemin-2(18)-glycyl-glycyl-l-histidine methyl ester (HGGH), and hemin-2,18-bis(glycyl-glycyl-l-histidine methyl ester) (H2GGH)—have been prepared by condensation of glycyl-l-histidine methyl ester or glycyl-glycyl-l-histidine methyl ester with the propionic side chains of hemin. Characterization by means of UV/vis- and 1H NMR spectroscopy as well as cyclic- and differential pulse voltammetry indicates the formation of five-coordinate complexes in the case of HGH and HGGH, with histidine as an axial ligand. In the case of H2GGH, a six-coordinate complex with both imidazoles coordinated to the iron center appears to be formed. However, 1H NMR of H2GGH reveals the existence of an equilibrium between low-spin six-coordinate and high-spin five-coordinate species in solution. The catalytic activity of the hemin–peptide complexes towards several organic substrates, such as p-cresol, l-tyrosine methyl ester, and ABTS, has been investigated. It was found that not only the five-coordinate HGH and HGGH complexes, but also the six-coordinate H2GGH, catalyze the oxidation of substrates by H2O2. The longer and less strained peptide arm provides the HGGH complex with a slightly higher catalytic efficiency, as compared with HGH, due to formation of more stable intermediate complexes. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Inorganic Chemistry
volume
9
issue
4
pages
385 - 395
publisher
Springer
external identifiers
  • pmid:15042435
  • wos:000221729500001
  • scopus:3042789507
ISSN
1432-1327
DOI
10.1007/s00775-004-0532-5
language
English
LU publication?
yes
id
81f8f213-0347-4a7f-a9d8-cc4322a6a969 (old id 141577)
date added to LUP
2007-07-09 14:12:54
date last changed
2017-08-13 03:44:24
@article{81f8f213-0347-4a7f-a9d8-cc4322a6a969,
  abstract     = {In order to create a heme environment that permits biomimicry of heme-containing peroxidases, a number of new hemin–peptide complexes—hemin-2(18)-glycyl-l-histidine methyl ester (HGH), hemin-2(18)-glycyl-glycyl-l-histidine methyl ester (HGGH), and hemin-2,18-bis(glycyl-glycyl-l-histidine methyl ester) (H2GGH)—have been prepared by condensation of glycyl-l-histidine methyl ester or glycyl-glycyl-l-histidine methyl ester with the propionic side chains of hemin. Characterization by means of UV/vis- and 1H NMR spectroscopy as well as cyclic- and differential pulse voltammetry indicates the formation of five-coordinate complexes in the case of HGH and HGGH, with histidine as an axial ligand. In the case of H2GGH, a six-coordinate complex with both imidazoles coordinated to the iron center appears to be formed. However, 1H NMR of H2GGH reveals the existence of an equilibrium between low-spin six-coordinate and high-spin five-coordinate species in solution. The catalytic activity of the hemin–peptide complexes towards several organic substrates, such as p-cresol, l-tyrosine methyl ester, and ABTS, has been investigated. It was found that not only the five-coordinate HGH and HGGH complexes, but also the six-coordinate H2GGH, catalyze the oxidation of substrates by H2O2. The longer and less strained peptide arm provides the HGGH complex with a slightly higher catalytic efficiency, as compared with HGH, due to formation of more stable intermediate complexes.},
  author       = {Ryabova, Ekaterina and Dikiy, Alexander and Hesslein, Ashley E and Bjerrum, Morten J and Ciurli, Stefano and Nordlander, Ebbe},
  issn         = {1432-1327},
  language     = {eng},
  number       = {4},
  pages        = {385--395},
  publisher    = {Springer},
  series       = {Journal of Biological Inorganic Chemistry},
  title        = {Preparation and reactivity studies of synthetic microperoxidases containing b-type heme},
  url          = {http://dx.doi.org/10.1007/s00775-004-0532-5},
  volume       = {9},
  year         = {2004},
}