Preparation and reactivity studies of synthetic microperoxidases containing b-type heme
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/141577
- author
- Ryabova, Ekaterina LU ; Dikiy, Alexander ; Hesslein, Ashley E ; Bjerrum, Morten J ; Ciurli, Stefano and Nordlander, Ebbe LU
- organization
- publishing date
- 2004
- 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
- 2016-04-01 12:24:34
- date last changed
- 2022-02-18 22:06:00
@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}}, doi = {{10.1007/s00775-004-0532-5}}, volume = {{9}}, year = {{2004}}, }