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Naji, M. |
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Motta, Antonella |
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Aletan, Dirar |
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Mohamed, Tarek |
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Ertürk, Emre |
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Taccardi, Nicola |
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Kononenko, Denys |
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Petrov, R. H. | Madrid |
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Alshaaer, Mazen | Brussels |
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Bih, L. |
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Casati, R. |
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Muller, Hermance |
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Kočí, Jan | Prague |
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Šuljagić, Marija |
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Kalteremidou, Kalliopi-Artemi | Brussels |
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Azam, Siraj |
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Ospanova, Alyiya |
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Blanpain, Bart |
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Ali, M. A. |
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Popa, V. |
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Rančić, M. |
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Ollier, Nadège |
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Azevedo, Nuno Monteiro |
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Landes, Michael |
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Rignanese, Gian-Marco |
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Wan, X.
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Publications (5/5 displayed)
- 2019Sequentially Deposited versus Conventional Nonfullerene Organic Solar Cells: Interfacial Trap States, Vertical Stratification, and Exciton Dissociationcitations
- 2018Correction: Efficient non-fullerene organic solar cells employing sequentially deposited donor-acceptor layers (Journal of Materials Chemistry A (2018) 6 (18225–18233) DOI: 10.1039/C8TA06860G)citations
- 2018Efficient non-fullerene organic solar cells employing sequentially deposited donor-acceptor layerscitations
- 2016High efficiency and stability small molecule solar cells developed by bulk microstructure fine-tuningcitations
- 2007Characterization of a globin-coupled oxygen sensor with a gene-regulating functioncitations
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article
Characterization of a globin-coupled oxygen sensor with a gene-regulating function
Abstract
Globin-coupled sensors (GCSs) are multiple-domain transducers,<sup> </sup>consisting of a regulatory globin-like heme-binding domain and<sup> </sup>a linked transducer domain(s). GCSs have been described in both<sup> </sup>Archaea and bacteria. They are generally assumed to bind O<sub>2</sub><sup> </sup>(and perhaps other gaseous ligands) and to transmit a conformational<sup> </sup>change signal through the transducer domain in response to fluctuating<sup> </sup>O<sub>2</sub> levels. In this study, the heme-binding domain, <em>Av</em>GReg178,<sup> </sup>and the full protein, <em>Av</em>GReg of the <em>Azotobacter vinelandii</em> GCS,<sup> </sup>were cloned, expressed, and purified. After purification, the<sup> </sup>heme iron of <em>Av</em>GReg178 was found to bind O<sub>2</sub>. This form was stable<sup> </sup>over many hours. In contrast, the predominant presence of a<sup> </sup>bis-histidine coordinate heme in ferric <em>Av</em>GReg was revealed.<sup> </sup>Differences in the heme pocket structure were also observed<sup> </sup>for the deoxygenated ferrous state of these proteins. The spectra<sup> </sup>showed that the deoxygenated ferrous derivatives of <em>Av</em>GReg178<sup> </sup>and <em>Av</em>GReg are characterized by a penta-coordinate and hexa-coordinate<sup> </sup>heme iron, respectively. O<sub>2</sub> binding isotherms indicate that<sup> </sup><em>Av</em>GReg178 and <em>Av</em>GReg show a high affinity for O<sub>2</sub> with <em>P</em><sub>50</sub> values<sup> </sup>at 20 °C of 0.04 and 0.15 torr, respectively. Kinetics of<sup> </sup>CO binding indicate that <em>Av</em>GReg178 carbonylation conforms to<sup> </sup>a monophasic process, comparable with that of myoglobin, whereas<sup> </sup><em>Av</em>GReg carbonylation conforms to a three-phasic reaction, as<sup> </sup>observed for several proteins with bis-histidine heme iron coordination.<sup> </sup>Besides sensing ligands, <em>in vitro</em> data suggest that <em>Av</em>GReg(178)<sup> </sup>may have a role in O<sub>2</sub>-mediated NO-detoxification, yielding met<em>Av</em>GReg(178)<sup> </sup>and nitrate.<sup> </sup>