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Title: Efficient reduction of CO 2 by the molybdenum-containing formate dehydrogenase from Cupriavidus necator ( Ralstonia eutropha )

Abstract

The ability of the FdsABG formate dehydrogenase from Cupriavidus necator (formerly known as Ralstonia eutropha) to catalyze the reverse of the physiological reaction, the reduction of CO2 to formate utilizing NADH as electron donor, has been investigated. Contrary to previous studies of this enzyme, we demonstrate that it is in fact effective in catalyzing the reverse reaction with a kcat of 11 ± 0.4 s−1. We also quantify the stoichiometric accumulation of formic acid as the product of the reaction and demonstrate that the observed kinetic parameters for catalysis in the forward and reverse reactions are thermodynamically consistent, complying with the expected Haldane relationships. Finally, we demonstrate the reaction conditions necessary for gauging the ability of a given formate dehydrogenase or other CO2-utilizing enzyme to catalyze the reverse direction to avoid false negative results. In conjunction with our earlier studies on the reaction mechanism of this enzyme and on the basis of the present work, we conclude that all molybdenum- and tungsten-containing formate dehydrogenases and related enzymes likely operate via a simple hydride transfer mechanism and are effective in catalyzing the reversible interconversion of CO2 and formate under the appropriate experimental conditions.

Authors:
; ; ;
Publication Date:
Research Org.:
Univ. of California, Riverside, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
1540306
Grant/Contract Number:  
SC0010666
Resource Type:
Accepted Manuscript
Journal Name:
Journal of Biological Chemistry
Additional Journal Information:
Journal Volume: 292; Journal Issue: 41; Journal ID: ISSN 0021-9258
Publisher:
American Society for Biochemistry and Molecular Biology
Country of Publication:
United States
Language:
English
Subject:
Biochemistry & Molecular Biology

Citation Formats

Yu, Xuejun, Niks, Dimitri, Mulchandani, Ashok, and Hille, Russ. Efficient reduction of CO 2 by the molybdenum-containing formate dehydrogenase from Cupriavidus necator ( Ralstonia eutropha ). United States: N. p., 2017. Web. doi:10.1074/jbc.m117.785576.
Yu, Xuejun, Niks, Dimitri, Mulchandani, Ashok, & Hille, Russ. Efficient reduction of CO 2 by the molybdenum-containing formate dehydrogenase from Cupriavidus necator ( Ralstonia eutropha ). United States. doi:10.1074/jbc.m117.785576.
Yu, Xuejun, Niks, Dimitri, Mulchandani, Ashok, and Hille, Russ. Mon . "Efficient reduction of CO 2 by the molybdenum-containing formate dehydrogenase from Cupriavidus necator ( Ralstonia eutropha )". United States. doi:10.1074/jbc.m117.785576. https://www.osti.gov/servlets/purl/1540306.
@article{osti_1540306,
title = {Efficient reduction of CO 2 by the molybdenum-containing formate dehydrogenase from Cupriavidus necator ( Ralstonia eutropha )},
author = {Yu, Xuejun and Niks, Dimitri and Mulchandani, Ashok and Hille, Russ},
abstractNote = {The ability of the FdsABG formate dehydrogenase from Cupriavidus necator (formerly known as Ralstonia eutropha) to catalyze the reverse of the physiological reaction, the reduction of CO2 to formate utilizing NADH as electron donor, has been investigated. Contrary to previous studies of this enzyme, we demonstrate that it is in fact effective in catalyzing the reverse reaction with a kcat of 11 ± 0.4 s−1. We also quantify the stoichiometric accumulation of formic acid as the product of the reaction and demonstrate that the observed kinetic parameters for catalysis in the forward and reverse reactions are thermodynamically consistent, complying with the expected Haldane relationships. Finally, we demonstrate the reaction conditions necessary for gauging the ability of a given formate dehydrogenase or other CO2-utilizing enzyme to catalyze the reverse direction to avoid false negative results. In conjunction with our earlier studies on the reaction mechanism of this enzyme and on the basis of the present work, we conclude that all molybdenum- and tungsten-containing formate dehydrogenases and related enzymes likely operate via a simple hydride transfer mechanism and are effective in catalyzing the reversible interconversion of CO2 and formate under the appropriate experimental conditions.},
doi = {10.1074/jbc.m117.785576},
journal = {Journal of Biological Chemistry},
number = 41,
volume = 292,
place = {United States},
year = {2017},
month = {8}
}

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Works referenced in this record:

Crystal Structure of Formate Dehydrogenase H: Catalysis Involving Mo, Molybdopterin, Selenocysteine, and an Fe4S4 Cluster
journal, February 1997

  • Boyington, Jeffrey C.; Gladyshev, Vadim N.; Khangulov, Sergei V.
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