Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Anabella Ivancich"'
Autor:
Anabella Ivancich, Olga Iranzo, Elisabeth Lojou, Barbara Schoepp-Cothenet, Karl J. Koebke, Borries Demeler, Vincent L. Pecoraro, Toni Kühl
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2021, 60 (8), pp.3974-3978. ⟨10.1002/anie.202012673⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2020, ⟨10.1002/anie.202012673⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2020, 60 (8), pp.3974-3978. ⟨10.1002/anie.202012673⟩
Angew Chem Int Ed Engl
Angewandte Chemie International Edition, 2021, 60 (8), pp.3974-3978. ⟨10.1002/anie.202012673⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2021, 60 (8), pp.3974-3978. ⟨10.1002/anie.202012673⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2020, ⟨10.1002/anie.202012673⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2020, 60 (8), pp.3974-3978. ⟨10.1002/anie.202012673⟩
Angew Chem Int Ed Engl
Angewandte Chemie International Edition, 2021, 60 (8), pp.3974-3978. ⟨10.1002/anie.202012673⟩
International audience; De Novo metalloprotein design assesses the relationship between metal active site architecture and catalytic reactivity. Herein, we use an alpha-helical scaffold to control the iron coordination geometry when a heme cofactor i
Publikováno v:
Chemical Science
Chemical Science, The Royal Society of Chemistry, 2020, 11 (10), pp.2681-2695. ⟨10.1039/c9sc04388h⟩
Chemical Science, 2020, 11 (10), pp.2681-2695. ⟨10.1039/c9sc04388h⟩
Chemical Science, The Royal Society of Chemistry, 2020, 11 (10), pp.2681-2695. ⟨10.1039/c9sc04388h⟩
Chemical Science, 2020, 11 (10), pp.2681-2695. ⟨10.1039/c9sc04388h⟩
Heme hydroperoxidases catalyze the oxidation of substrates by H2O2. The catalytic cycle involves the formation of a highly oxidizing species known as Compound I, resulting from the two-electron oxidation of the ferric heme in the active site of the r
Autor:
Anabella Ivancich, Peter C. Loewen
Publikováno v:
Encyclopedia of Biophysics ISBN: 9783642359439
Encyclopedia of Biophysics
Encyclopedia of Biophysics, 2018, 978-3-642-35943-9. ⟨10.1007/978-3-642-35943-9_51-1⟩
Encyclopedia of Biophysics
Encyclopedia of Biophysics, 2018, 978-3-642-35943-9. ⟨10.1007/978-3-642-35943-9_51-1⟩
International audience; Catalases (EC 1.11.1.6) are enzymes that catalyze the disproportionation of hydrogen peroxide into water and molecular oxygen by means of a heme iron or a dimanganese active site. They are crucial metalloproteins regulating th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fcb6108c6ef2d00e033f219d4ba2316
https://doi.org/10.1007/978-3-642-35943-9_51-1
https://doi.org/10.1007/978-3-642-35943-9_51-1
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 83:853-866
Heme-containing catalases and catalase-peroxidases catalyze the dismutation of hydrogen peroxide as their predominant catalytic activity, but in addition, individual enzymes support low levels of peroxidase and oxidase activities, produce superoxide,
Autor:
Anabella Ivancich, Lynda J. Donald, Nadime Karaduman, Parisa Hosseinzadeh, Yi Lu, Peter C. Loewen, Thomas D. Pfister, Kyle D. Miner
Publikováno v:
Biochemistry
Biochemistry, 2014, 53 (23), pp.3781-3789. ⟨10.1021/bi500353p⟩
Biochemistry, American Chemical Society, 2014, 53 (23), pp.3781-3789. ⟨10.1021/bi500353p⟩
Biochemistry, 2014, 53 (23), pp.3781-3789. ⟨10.1021/bi500353p⟩
Biochemistry, American Chemical Society, 2014, 53 (23), pp.3781-3789. ⟨10.1021/bi500353p⟩
International audience; The location of the Trp radical and the catalytic function of the [Fe(IV)═O Trp191•+] intermediate in cytochrome c peroxidase (CcP) are well-established; however, the unambiguous identification of the site(s) for the forma
Autor:
Anabella Ivancich, Peter C. Loewen, Lynda J. Donald, Ignacio Fita, Jacylyn Villanueva, Ben Wiseman
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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Catalase-peroxidases or KatGs can utilize organic peroxyacids and peroxides instead of hydrogen peroxide to generate the high-valent ferryl-oxo intermediates involved in the catalase and peroxidase reactions. In the absence of peroxidatic one-electro
Publikováno v:
Biochemistry. 49:8857-8872
We have identified a novel enzymatic reaction for nitrophorin 2 (NP2), a heme protein previously characterized as a nitric oxide carrier in the saliva of the Rhodnius prolixus insect. NP2 exhibited levels of peroxidase activity comparable to those of
Publikováno v:
Proceedings of the National Academy of Sciences. 106:16084-16089
The surface oxidation site (Trp-171) in lignin peroxidase (LiP) required for the reaction with veratryl alcohol a high-redox-potential (1.4 V) substrate, was engineered into Coprinus cinereus peroxidase (CiP) by introducing a Trp residue into a heme
Autor:
Elena M. Ghibaudi, Anabella Ivancich, Alistair J. Fielding, Barbara Boscolo, Peter C. Loewen, Rahul Singh
Publikováno v:
Biochemistry. 47:9781-9792
We have combined the information obtained from rapid-scan electronic absorption spectrophotometry and multifrequency (9-295 GHz) electron paramagnetic resonance (EPR) spectroscopy to unequivocally determine the electronic nature of the intermediates
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 12:233-240