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Title: 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 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.
Authors:
 [1] ;  [1] ;  [1] ;  [2] ;  [3] ;  [2] ;  [2] ;  [3] ;  [4] ; ORCiD logo [1]
  1. Univ. Grenoble Alpes, Grenoble Cedex (France)
  2. Argonne National Lab. (ANL), Lemont, IL (United States)
  3. Tohoku Univ., Sendai (Japan)
  4. Univ. Grenoble Alpes, Grenoble Cedex (France); Univ. Pierre et Marie Curie, Paris (France)
Publication Date:
Grant/Contract Number:
AC02-06CH11357; AC02-6CH11357; 2412006; 24350081; 23550186; 25109504; 15K05555; 15H00912
Type:
Accepted Manuscript
Journal Name:
ChemPlusChem
Additional Journal Information:
Journal Volume: 81; Journal Issue: 10; Journal ID: ISSN 2192-6506
Publisher:
ChemPubSoc Europe
Research Org:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; biohybrid species; hydrogen evolution; artificial enzymes; bioinspired chemistry; cobalt; heme proteins; enzyme models; biohybrids
OSTI Identifier:
1351308
Alternate Identifier(s):
OSTI ID: 1401439

Bacchi, Marine, Veinberg, Elias, Field, Martin J., Niklas, Jens, Matsui, Toshitaka, Tiede, David M., Poluektov, Oleg G., Ikeda-Saito, Masao, Fontecave, Marc, and Artero, Vincent. Artificial hydrogenases based on cobaloximes and heme oxygenase. United States: N. p., Web. doi:10.1002/cplu.201600218.
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. United States. doi:10.1002/cplu.201600218.
Bacchi, Marine, Veinberg, Elias, Field, Martin J., Niklas, Jens, Matsui, Toshitaka, Tiede, David M., Poluektov, Oleg G., Ikeda-Saito, Masao, Fontecave, Marc, and Artero, Vincent. 2016. "Artificial hydrogenases based on cobaloximes and heme oxygenase". United States. doi:10.1002/cplu.201600218. https://www.osti.gov/servlets/purl/1351308.
@article{osti_1351308,
title = {Artificial hydrogenases based on cobaloximes and heme oxygenase},
author = {Bacchi, Marine and Veinberg, Elias and Field, Martin J. and Niklas, Jens and Matsui, Toshitaka and Tiede, David M. and Poluektov, Oleg G. and Ikeda-Saito, Masao and Fontecave, Marc and Artero, Vincent},
abstractNote = {The insertion of cobaloxime catalysts in the heme-binding pocket of heme oxygenase (HO) yields artificial hydrogenases active for H2 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} (dmgH2 = 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.},
doi = {10.1002/cplu.201600218},
journal = {ChemPlusChem},
number = 10,
volume = 81,
place = {United States},
year = {2016},
month = {6}
}