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Engineering of formate dehydrogenase for improving conversion potential of carbon dioxide to formate
by
Tang, Cun-Duo
, Yuan, Shu-Wei
, Xi, Xiao-Qi
, Yue, Chao
, Shi, Hong-Ling
, Xie, Yu-Li
, Zhang, Ying-Jun
, Xue, Chuang
, Yao, Lun-Guang
in
Biochemical characteristics
/ Biochemistry
/ Carbon dioxide
/ Dehydrogenase
/ Dehydrogenases
/ Formate dehydrogenase
/ Hydroxy acids
/ Mutants
/ Reductases
/ Reduction
2023
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Engineering of formate dehydrogenase for improving conversion potential of carbon dioxide to formate
by
Tang, Cun-Duo
, Yuan, Shu-Wei
, Xi, Xiao-Qi
, Yue, Chao
, Shi, Hong-Ling
, Xie, Yu-Li
, Zhang, Ying-Jun
, Xue, Chuang
, Yao, Lun-Guang
in
Biochemical characteristics
/ Biochemistry
/ Carbon dioxide
/ Dehydrogenase
/ Dehydrogenases
/ Formate dehydrogenase
/ Hydroxy acids
/ Mutants
/ Reductases
/ Reduction
2023
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Engineering of formate dehydrogenase for improving conversion potential of carbon dioxide to formate
by
Tang, Cun-Duo
, Yuan, Shu-Wei
, Xi, Xiao-Qi
, Yue, Chao
, Shi, Hong-Ling
, Xie, Yu-Li
, Zhang, Ying-Jun
, Xue, Chuang
, Yao, Lun-Guang
in
Biochemical characteristics
/ Biochemistry
/ Carbon dioxide
/ Dehydrogenase
/ Dehydrogenases
/ Formate dehydrogenase
/ Hydroxy acids
/ Mutants
/ Reductases
/ Reduction
2023
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Engineering of formate dehydrogenase for improving conversion potential of carbon dioxide to formate
Journal Article
Engineering of formate dehydrogenase for improving conversion potential of carbon dioxide to formate
2023
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Overview
Formate dehydrogenase (FDH) is a D-2-hydroxy acid dehydrogenase, which can reversibly reduce CO2 to formate and thus act as non-photosynthetic CO2 reductase. In order to increase catalytic efficiency of formate dehydrogenase for CO2 reduction, two mutants V328I/F285W and V354G/F285W were obtained of which reduction activity was about two times more than the parent CbFDHM2, and the formate production from CO2 catalyzed by mutants were 2.9 and 2.7-fold higher than that of the parent CbFDHM2. The mutants had greater potential in CO2 reduction. The optimal temperature for V328I/F285W and V354G/F285W was 55 °C, and they showed increasement of relative activity under 45 °C to 55 °C compared with parent. The optimal pH for the mutants was 9.0, and they showed excellent stability in pH 4.0–11.5. The kcat/Km values of mutants were 1.75 times higher than that of the parent. Then the molecular basis for its improvement of biochemical characteristics were preliminarily elucidated by computer-aided methods. All of these results further established a solid foundation for molecular modification of formate dehydrogenase and CO2 reduction.
Publisher
Springer Nature B.V
Subject
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