Artificial hydrogenases based on cobaloximes and heme oxygenase
The insertion of cobaloxime catalysts in the heme-binding pocket of heme oxygenase (HO) yields artificial hydrogenases active for H 2 evolution in neutral aqueous solutions. These novel biohybrids have been purified and characterized by using UV/visible and EPR spectroscopy. These analyses revealed...
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ftosti:oai:osti.gov:1351308 2023-07-30T04:07:06+02:00 Artificial hydrogenases based on cobaloximes and heme oxygenase Bacchi, Marine Veinberg, Elias Field, Martin J. Niklas, Jens Matsui, Toshitaka Tiede, David M. Poluektov, Oleg G. Ikeda-Saito, Masao Fontecave, Marc Artero, Vincent 2021-07-23 application/pdf http://www.osti.gov/servlets/purl/1351308 https://www.osti.gov/biblio/1351308 https://doi.org/10.1002/cplu.201600218 unknown http://www.osti.gov/servlets/purl/1351308 https://www.osti.gov/biblio/1351308 https://doi.org/10.1002/cplu.201600218 doi:10.1002/cplu.201600218 37 INORGANIC ORGANIC PHYSICAL AND ANALYTICAL CHEMISTRY 2021 ftosti https://doi.org/10.1002/cplu.201600218 2023-07-11T09:18:05Z The insertion of cobaloxime catalysts in the heme-binding pocket of heme oxygenase (HO) yields artificial hydrogenases active for H 2 evolution in neutral aqueous solutions. These novel biohybrids have been purified and characterized by using UV/visible and EPR spectroscopy. These analyses revealed the presence of two distinct binding conformations, thereby providing the cobaloxime with hydrophobic and hydrophilic environments, respectively. Quantum chemical/molecular mechanical docking calculations found open and closed conformations of the binding pocket owing to mobile amino acid residues. HO-based biohybrids incorporating a {Co(dmgH) 2 } (dmgH 2 = dimethylglyoxime) catalytic center displayed up to threefold increased turnover numbers with respect to the cobaloxime alone or to analogous sperm whale myoglobin adducts. Here, this study thus provides a strong basis for further improvement of such biohybrids, using well-designed modifications of the second and outer coordination spheres, through site-directed mutagenesis of the host protein. Other/Unknown Material Sperm whale SciTec Connect (Office of Scientific and Technical Information - OSTI, U.S. Department of Energy) ChemPlusChem 81 10 1083 1089 |
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SciTec Connect (Office of Scientific and Technical Information - OSTI, U.S. Department of Energy) |
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37 INORGANIC ORGANIC PHYSICAL AND ANALYTICAL CHEMISTRY |
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37 INORGANIC ORGANIC PHYSICAL AND ANALYTICAL CHEMISTRY Bacchi, Marine Veinberg, Elias Field, Martin J. Niklas, Jens Matsui, Toshitaka Tiede, David M. Poluektov, Oleg G. Ikeda-Saito, Masao Fontecave, Marc Artero, Vincent Artificial hydrogenases based on cobaloximes and heme oxygenase |
topic_facet |
37 INORGANIC ORGANIC PHYSICAL AND ANALYTICAL CHEMISTRY |
description |
The insertion of cobaloxime catalysts in the heme-binding pocket of heme oxygenase (HO) yields artificial hydrogenases active for H 2 evolution in neutral aqueous solutions. These novel biohybrids have been purified and characterized by using UV/visible and EPR spectroscopy. These analyses revealed the presence of two distinct binding conformations, thereby providing the cobaloxime with hydrophobic and hydrophilic environments, respectively. Quantum chemical/molecular mechanical docking calculations found open and closed conformations of the binding pocket owing to mobile amino acid residues. HO-based biohybrids incorporating a {Co(dmgH) 2 } (dmgH 2 = dimethylglyoxime) catalytic center displayed up to threefold increased turnover numbers with respect to the cobaloxime alone or to analogous sperm whale myoglobin adducts. Here, this study thus provides a strong basis for further improvement of such biohybrids, using well-designed modifications of the second and outer coordination spheres, through site-directed mutagenesis of the host protein. |
author |
Bacchi, Marine Veinberg, Elias Field, Martin J. Niklas, Jens Matsui, Toshitaka Tiede, David M. Poluektov, Oleg G. Ikeda-Saito, Masao Fontecave, Marc Artero, Vincent |
author_facet |
Bacchi, Marine Veinberg, Elias Field, Martin J. Niklas, Jens Matsui, Toshitaka Tiede, David M. Poluektov, Oleg G. Ikeda-Saito, Masao Fontecave, Marc Artero, Vincent |
author_sort |
Bacchi, Marine |
title |
Artificial hydrogenases based on cobaloximes and heme oxygenase |
title_short |
Artificial hydrogenases based on cobaloximes and heme oxygenase |
title_full |
Artificial hydrogenases based on cobaloximes and heme oxygenase |
title_fullStr |
Artificial hydrogenases based on cobaloximes and heme oxygenase |
title_full_unstemmed |
Artificial hydrogenases based on cobaloximes and heme oxygenase |
title_sort |
artificial hydrogenases based on cobaloximes and heme oxygenase |
publishDate |
2021 |
url |
http://www.osti.gov/servlets/purl/1351308 https://www.osti.gov/biblio/1351308 https://doi.org/10.1002/cplu.201600218 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_relation |
http://www.osti.gov/servlets/purl/1351308 https://www.osti.gov/biblio/1351308 https://doi.org/10.1002/cplu.201600218 doi:10.1002/cplu.201600218 |
op_doi |
https://doi.org/10.1002/cplu.201600218 |
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ChemPlusChem |
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81 |
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10 |
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1083 |
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1089 |
_version_ |
1772820210713100288 |