Zobrazeno 1 - 10 of 33 pro vyhledávání: '"G W, Canters"'
1
Bidirectional Catalysis by Copper-Containing Nitrite Reductase
Autor: Martin Ph. Verbeet, G. W. Canters, Simon de Vries, Hein J. Wijma
Publikováno v: Biochemistry, 43(32), 10467-10474. AMER CHEMICAL SOC
The copper-containing nitrite reductase from Alcaligenes faecalis S-6 was found to catalyze the oxidation of nitric oxide to nitrite, the reverse of its physiological reaction. Thermodynamic and kinetic constants with the physiological electron donor
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2d6161d48f3202b5031d7eb20288692
https://doi.org/10.1021/bi0496687
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2
Solid state protein monolayers: morphological, conformational, and funcional properties
Autor: P. P. POMPA, A. BIASCO, V. FRASCERRA, F. CALABI, M. P. VERBET, E. DE WAAL, G. W. CANTERS, CINGOLANI, Roberto, RINALDI, Rosaria
We have studied the morphological, conformational, and electron-transfer (ET) function of the metalloprotein azurin in the solid state, by a combination of physical investigation methods, namely atomic force microscopy, intrinsic fluorescence spectro
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______4034::f397296484802c990af4d0dbd2899144
https://hdl.handle.net/11587/300542
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3
Electronic rectification in protein devices
Autor: M. Ph. Verbeet, Paolo Facci, A. Biasco, R. Cingolani, Giuseppe Maruccio, F. De Rienzo, G. W. Canters, R. Di Felice, Elisa Molinari, Valentina Arima, Paolo Visconti, Ross Rinaldi
Publikováno v: Applied physics letters (Online) 82 (2003): 472.
info:cnr-pdr/source/autori:R. Rinaldi, A. Biasco, G. Maruccio, V. Arima, P. Visconti,R. Cingolani, P. Facci, F. De Rienzo, R. Di Felice, and E. Molinari, M. Ph. Verbeet and G. W. Canters/titolo:Electronic rectification in protein devices/doi:/rivista:Applied physics letters (Online)/anno:2003/pagina_da:472/pagina_a:/intervallo_pagine:472/volume:82
We show that the electron-transfer protein azurin can be used to fabricate biomolecular rectifiers exploiting its native redox properties, chemisorption capability and electrostatic features. The devices consist of a protein layer interconnecting nan
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4581fc68928d8267188a6649235ff9ac
https://hdl.handle.net/11587/107353
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4
Redox cycling and kinetic analyses of single molecules of solution-phase nitrite reductase
Autor: Thijs J. Aartsma, Leandro C. Tabares, Dorota Kostrz, Christopher Dennison, G. W. Canters, Randall H. Goldsmith, W. E. Moerner
Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 108(42), 17269-17274
Single-molecule measurements are a valuable tool for revealing details of enzyme mechanisms by enabling observation of unsynchronized behavior. However, this approach often requires immobilizing the enzyme on a substrate, a process which may alter en
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::373250a40f99bcdb1c4445d5f5002227
https://doi.org/10.1073/pnas.1113572108
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5
Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partially oxidised samples
Autor: J, Salgado, A P, Kalverda, G W, Canters
Publikováno v: Journal of biomolecular NMR. 9(3)
The relaxation enhancement caused by paramagnetic copper(II) is used to observe selectivelythe metal site of copper(I)-amicyanin by one- and two-dimensional NMR spectroscopy. Theparamagnetic effect is communicated to the diamagnetic protein through t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d07c00da78b59caa8404bdd3c066ac2c
https://pubmed.ncbi.nlm.nih.gov/20680661
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6
The importance of Asn47 for structure and reactivity of azurin from Alcaligenes denitrificans as studied by site-directed mutagenesis and spectroscopy
Autor: G. W. Canters, C. W. G. Hoitink
Publikováno v: Journal of Biological Chemistry. 267:13836-13842
To study the importance of a rigid copper site for the structure and function of azurin, a mutant with a reduced number of internal hydrogen bonds around the copper has been prepared and characterized. To this purpose, the previously cloned azu gene
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9a20eb131528ca8501983cf91bf5d3a8
https://doi.org/10.1016/s0021-9258(19)49644-0
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8
The structural homology of amicyanin from Thiobacillus versutus to plant plastocyanins
Autor: A Lommen, S M Van Bun, C Chothia, J. Van Beeumen, G W Canters
Publikováno v: Journal of Biological Chemistry. 266:4869-4877
The complete amino acid sequence of the blue copper protein amicyanin of Thiobacillus versutus, induced when the bacterium is grown on methylamine, has been determined as follows: QDKITVTSEKPVAAADVPADAVVVGIEKMKYLTPEVTIKAGETVYWVNGEVMPHNVA FKKGIVGEDAFR
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3a3a01233164cb8202ce2c0534b92a3
https://doi.org/10.1016/s0021-9258(19)67729-x
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10
Protein film voltammetry of copper-containing nitrite reductase reveals reversible inactivation
Autor: Lars J. C. Jeuken, Fraser A. Armstrong, G. W. Canters, Hein J. Wijma, Martin Ph. Verbeet
Publikováno v: Journal of the American Chemical Society, 129(27), 8557-8565. AMER CHEMICAL SOC
The Cu-containing nitrite reductase from Alcaligenes faecalis S-6 catalyzes the one-electron reduction of nitrite to nitric oxide (NO). Electrons enter the enzyme at the so-called type-1 Cu site and are then transferred internally to the catalytic ty
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cb65da972851949ddcf247da40f3f5d
https://pubmed.ncbi.nlm.nih.gov/17579406
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