Direct detection of a single [4Fe‐4S] cluster in a tungsten‐containing enzyme: Electrochemical conversion of CO2 into formate by formate dehydrogenase
Abstract The conversion of CO2 into fuels and valuable chemicals is one of the central topics to combat climate change and meet the growing demand for renewable energy. Herein, we show that the formate dehydrogenase from Clostridium ljungdahlii (ClFDH) adsorbed on electrodes displays clear character...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2023-05-01
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| Series: | Carbon Energy |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/cey2.304 |
| _version_ | 1797814209691516928 |
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| author | Wenjin Li Yanxin Gao Xuan Sun Lei Wan Haishuo Ji Hang Luo Yao Tian Hao Song Geng Wu Liyun Zhang |
| author_facet | Wenjin Li Yanxin Gao Xuan Sun Lei Wan Haishuo Ji Hang Luo Yao Tian Hao Song Geng Wu Liyun Zhang |
| author_sort | Wenjin Li |
| collection | DOAJ |
| description | Abstract The conversion of CO2 into fuels and valuable chemicals is one of the central topics to combat climate change and meet the growing demand for renewable energy. Herein, we show that the formate dehydrogenase from Clostridium ljungdahlii (ClFDH) adsorbed on electrodes displays clear characteristic voltammetric signals that can be assigned to the reduction and oxidation potential of the [4Fe‐4S]2+/+ cluster under nonturnover conditions. Upon adding substrates, the signals transform into a specific redox center that engages in catalytic electron transport. ClFDH catalyzes rapid and efficient reversible interconversion between CO2 and formate in the presence of substrates. The turnover frequency of electrochemical CO2 reduction is determined as 1210 s−1 at 25 °C and pH 7.0, which can be further enhanced up to 1786 s−1 at 50°C. The Faradaic efficiency at −0.6 V (vs. standard hydrogen electrode) is recorded as 99.3% in a 2‐h reaction. Inhibition experiments and theoretical modeling disclose interesting pathways for CO2 entry, formate exit, and OCN− competition, suggesting an oxidation‐state‐dependent binding mechanism of catalysis. Our results provide a different perspective for understanding the catalytic mechanism of FDH and original insights into the design of synthetic catalysts. |
| first_indexed | 2024-03-13T08:04:14Z |
| format | Article |
| id | doaj.art-69f2b4afd9df46f0be5ab0fa075c896a |
| institution | Directory Open Access Journal |
| issn | 2637-9368 |
| language | English |
| last_indexed | 2024-03-13T08:04:14Z |
| publishDate | 2023-05-01 |
| publisher | Wiley |
| record_format | Article |
| series | Carbon Energy |
| spelling | doaj.art-69f2b4afd9df46f0be5ab0fa075c896a2023-06-01T08:22:36ZengWileyCarbon Energy2637-93682023-05-0155n/an/a10.1002/cey2.304Direct detection of a single [4Fe‐4S] cluster in a tungsten‐containing enzyme: Electrochemical conversion of CO2 into formate by formate dehydrogenaseWenjin Li0Yanxin Gao1Xuan Sun2Lei Wan3Haishuo Ji4Hang Luo5Yao Tian6Hao Song7Geng Wu8Liyun Zhang9State Key Laboratory of Medicinal Chemical Biology, College of Life Science Nankai University Tianjin People's Republic of ChinaState Key Laboratory of Medicinal Chemical Biology, College of Life Science Nankai University Tianjin People's Republic of ChinaState Key Laboratory of Microbial Metabolism, The Joint International Research Laboratory of Metabolic & Developmental Sciences, School of Life Science and Biotechnology Shanghai Jiao Tong University Shanghai People's Republic of ChinaMax Planck Institute for Chemical Energy Conversion Mülheim an der Ruhr GermanyState Key Laboratory of Medicinal Chemical Biology, College of Life Science Nankai University Tianjin People's Republic of ChinaState Key Laboratory of Medicinal Chemical Biology, College of Life Science Nankai University Tianjin People's Republic of ChinaFrontier Science Center for Synthetic Biology, Key Laboratory of Systems Bioengineering, School of Chemical Engineering and Technology Tianjin University Tianjin People's Republic of ChinaFrontier Science Center for Synthetic Biology, Key Laboratory of Systems Bioengineering, School of Chemical Engineering and Technology Tianjin University Tianjin People's Republic of ChinaState Key Laboratory of Microbial Metabolism, The Joint International Research Laboratory of Metabolic & Developmental Sciences, School of Life Science and Biotechnology Shanghai Jiao Tong University Shanghai People's Republic of ChinaState Key Laboratory of Medicinal Chemical Biology, College of Life Science Nankai University Tianjin People's Republic of ChinaAbstract The conversion of CO2 into fuels and valuable chemicals is one of the central topics to combat climate change and meet the growing demand for renewable energy. Herein, we show that the formate dehydrogenase from Clostridium ljungdahlii (ClFDH) adsorbed on electrodes displays clear characteristic voltammetric signals that can be assigned to the reduction and oxidation potential of the [4Fe‐4S]2+/+ cluster under nonturnover conditions. Upon adding substrates, the signals transform into a specific redox center that engages in catalytic electron transport. ClFDH catalyzes rapid and efficient reversible interconversion between CO2 and formate in the presence of substrates. The turnover frequency of electrochemical CO2 reduction is determined as 1210 s−1 at 25 °C and pH 7.0, which can be further enhanced up to 1786 s−1 at 50°C. The Faradaic efficiency at −0.6 V (vs. standard hydrogen electrode) is recorded as 99.3% in a 2‐h reaction. Inhibition experiments and theoretical modeling disclose interesting pathways for CO2 entry, formate exit, and OCN− competition, suggesting an oxidation‐state‐dependent binding mechanism of catalysis. Our results provide a different perspective for understanding the catalytic mechanism of FDH and original insights into the design of synthetic catalysts.https://doi.org/10.1002/cey2.304bioelectrocatalysisbiofuelCO2 conversionformate dehydrogenaseiron–sulfur cluster |
| spellingShingle | Wenjin Li Yanxin Gao Xuan Sun Lei Wan Haishuo Ji Hang Luo Yao Tian Hao Song Geng Wu Liyun Zhang Direct detection of a single [4Fe‐4S] cluster in a tungsten‐containing enzyme: Electrochemical conversion of CO2 into formate by formate dehydrogenase Carbon Energy bioelectrocatalysis biofuel CO2 conversion formate dehydrogenase iron–sulfur cluster |
| title | Direct detection of a single [4Fe‐4S] cluster in a tungsten‐containing enzyme: Electrochemical conversion of CO2 into formate by formate dehydrogenase |
| title_full | Direct detection of a single [4Fe‐4S] cluster in a tungsten‐containing enzyme: Electrochemical conversion of CO2 into formate by formate dehydrogenase |
| title_fullStr | Direct detection of a single [4Fe‐4S] cluster in a tungsten‐containing enzyme: Electrochemical conversion of CO2 into formate by formate dehydrogenase |
| title_full_unstemmed | Direct detection of a single [4Fe‐4S] cluster in a tungsten‐containing enzyme: Electrochemical conversion of CO2 into formate by formate dehydrogenase |
| title_short | Direct detection of a single [4Fe‐4S] cluster in a tungsten‐containing enzyme: Electrochemical conversion of CO2 into formate by formate dehydrogenase |
| title_sort | direct detection of a single 4fe 4s cluster in a tungsten containing enzyme electrochemical conversion of co2 into formate by formate dehydrogenase |
| topic | bioelectrocatalysis biofuel CO2 conversion formate dehydrogenase iron–sulfur cluster |
| url | https://doi.org/10.1002/cey2.304 |
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