Review
Chemistry, Multidisciplinary
Marta Meneghello, Christophe Leger, Vincent Fourmond
Summary: Only two enzymes, CO dehydrogenase and formate dehydrogenase, are capable of directly reducing CO2, producing CO and formate respectively. These metalloenzymes are rapid, energy-efficient, and specific in product. Researchers have studied their mechanisms using protein film electrochemistry, and also exploited their catalytic performance to build biotechnological devices.
CHEMISTRY-A EUROPEAN JOURNAL
(2021)
Article
Chemistry, Physical
Mihai-Cristian Fera, Rita R. Manuel, Ines A. C. Pereira, Jose M. Abad, Antonio L. De Lacey, Marcos Pita
Summary: The electrochemical reduction of CO2 through redox enzymes is a promising method to reduce global CO2 concentrations. In this study, the enzyme Desulfovibrio vulgaris Hildenborough FdhAB formate dehydrogenase was effectively immobilized on MWCNTs-modified low density graphite electrodes using electrostatic interactions and protected with polyethyleneimine (PEI) polymer. The synergistic effect of MWCNTs and PEI resulted in high catalytic current densities and long-term operational stability.
Review
Chemistry, Multidisciplinary
Cristhian Molina-Fernandez, Patricia Luis
Summary: The use of immobilized carbonic anhydrase as a novel approach for CO2 capture presents a promising alternative to address cost and environmental issues. Current research focuses on developing different carriers and immobilization strategies to achieve stability and activity compared to free enzyme in solution.
JOURNAL OF CO2 UTILIZATION
(2021)
Article
Biotechnology & Applied Microbiology
Jiabao Xv, Zeyang Zhang, Saizhao Pang, Jiahui Jia, Zixin Geng, Ruirui Wang, Peikun Li, Muhammad Bilal, Jiandong Cui, Shiru Jia
Summary: This study improves the CO2 capture capacity of immobilized carbonic anhydrase (CA) by modifying a metal-organic framework MOF-808. The immobilized CA@PEI/PDA-MOF-808 exhibits significantly enhanced CO2 capture capacity and stability compared to free CA and modified MOF-808.
BIOCHEMICAL ENGINEERING JOURNAL
(2022)
Editorial Material
Plant Sciences
Justin Findinier, Arthur R. Grossman
Summary: The CO2-concentrating mechanism is an inorganic carbon pump used by eukaryotic algae to promote carbon fixation. It has the potential to be transferred to crop species, enhancing agricultural yields and supporting a growing world population.
JOURNAL OF EXPERIMENTAL BOTANY
(2023)
Review
Biochemistry & Molecular Biology
Rocio Villa, Susana Nieto, Antonio Donaire, Pedro Lozano
Summary: Direct biocatalytic processes for CO2 capture and transformation are effective tools for reducing greenhouse gas concentration. Carbonic anhydrase and formate dehydrogenase are two key enzymes that facilitate CO2 uptake and conversion into valuable chemicals.
Article
Limnology
Youting Ye, William G. Sunda, Haizheng Hong, Dalin Shi
Summary: The study suggests that increasing seawater CO2 concentrations may enhance the carbon fixation rates in Fe- and light-limited and co-limited regions, leading to a decrease in energy demands and oxidative stress for marine phytoplankton.
LIMNOLOGY AND OCEANOGRAPHY
(2022)
Article
Chemistry, Multidisciplinary
Ferran Esteve, Fidan Rahmatova, Jean-Marie Lehn
Summary: This study reveals the remarkable effect of supramolecular multivalency on increasing imine stability. By synthesizing a series of reactive aldehydes bearing supramolecularly-active sites, it was found that decreasing the degree of supramolecular multivalency significantly decreased imine yields. Preliminary results on protein bioconjugation demonstrated the ability to dynamically inhibit the activity of carbonic anhydrase and recover its initial activity with a suitable chemical effector.
Article
Green & Sustainable Science & Technology
Shan Chang, Yan He, Yinxi Li, Xuemin Cui
Summary: This study focused on immobilizing carbonic anhydrases on geopolymer microspheres for CO2 capture and sequestration. Optimal conditions included pH 8.0, temperature 30 degrees C, and incubation for 2 hours. The immobilized enzyme showed improved thermal and storage stability compared to the free enzyme.
JOURNAL OF CLEANER PRODUCTION
(2021)
Article
Biochemistry & Molecular Biology
Franziska Steger, Johanna Reich, Werner Fuchs, Simon K. -M. R. Rittmann, Georg M. Guebitz, Doris Ribitsch, Guenther Bochmann
Summary: Strategies for depleting carbon dioxide (CO2) from flue gases are urgently needed, and carbonic anhydrases (CAs) can contribute to solving this problem. This current study examines four recombinantly produced CAs from different organisms, namely CAs from Acetobacterium woodii (AwCA or CynT), Persephonella marina (PmCA), Methanobacterium thermoautotrophicum (MtaCA or Cab), and Sulphurihydrogenibium yellowstonense (SspCA). The highest expression yields and activities were found for AwCA and PmCA. AwCA showed high stability in a mesophilic temperature range, while PmCA proved to be exceptionally thermostable. These results indicate the potential to utilize CAs from anaerobic microorganisms for CO2 sequestration applications.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Biophysics
Sizhu Ren, Ruixue Chen, Zhangfei Wu, Shan Su, Jiaxi Hou, Yanlin Yuan
Summary: The immobilization of CA is crucial in enhancing enzyme stability and utilization, but the choice of immobilization methods and conditions must be carefully considered to prevent a decrease in CA activity and impact on CO2 conversion. Immobilized CA has promising applications in the environmental sector, particularly in CO2 mineralization and multienzyme cascade catalysis.
COLLOIDS AND SURFACES B-BIOINTERFACES
(2021)
Article
Environmental Sciences
Tanvi Sharma, Abhishek Sharma, Chang lei Xia, Su Shiung Lam, Azmat Ali Khan, Sonam Tripathi, Raj Kumar, Vijai Kumar Gupta, Ashok Kumar Nadda
Summary: In this study, a bacterial carbonic anhydrase (CA) was purified and used to convert CO2 into CaCO3. The purified CA showed optimal activity at 35 degrees C and pH 7.5, and exhibited good efficacy in converting CO2 into CaCO3. The study also provided insights into the structure and binding site of the purified CA.
ENVIRONMENTAL RESEARCH
(2022)
Review
Biochemistry & Molecular Biology
Jialong Shen, Sonja Salmon
Summary: Innovative carbon capture technologies are needed to combat climate change, including technologies that can capture CO2 from large sources and directly from the air. The captured CO2 can be converted into valuable chemical feedstocks and products, replacing fossil-based materials for a renewable economy. The use of biocatalytic membranes, which combine high reaction rates and enzyme selectivity, shows promise for both capturing and utilizing CO2. This review examines technologies under development that employ enzymes and membranes for CO2 capture and utilization, discussing progress, challenges, and future research directions.
Review
Environmental Sciences
Xing Zhu, Chenxi Du, Bo Gao, Bin He
Summary: High carbon dioxide concentration in the atmosphere calls for eco-friendly mitigation strategies. Carbonic anhydrase (CA) immobilization can enhance its stability and enzyme recycling, but there is limited mass transfer between gaseous CO2 and the active center of immobilized CA. This review focuses on improving the mass transfer process to increase the efficiency of enzymatic CO2 capture for industrial applications.
JOURNAL OF ENVIRONMENTAL MANAGEMENT
(2023)
Article
Plant Sciences
Pengpeng Li, Zuying Liao, Jingzhe Zhou, Liyan Yin, Hong Sheng Jiang, Wei Li
Summary: Submerged macrophytes have developed the ability to use bicarbonate to mitigate the effects of photorespiration, leading to increased oxygen production. Experiments have shown that inhibiting bicarbonate use with a carbonic anhydrase inhibitor significantly reduces oxygen production rate in three out of four studied submerged macrophytes, while the species that solely use CO2 are not affected.
ENVIRONMENTAL AND EXPERIMENTAL BOTANY
(2021)
Article
Chemistry, Multidisciplinary
Marta Meneghello, Alexandre Uzel, Marianne Broc, Rita R. Manuel, Axel Magalon, Christophe Leger, Ines A. C. Pereira, Anne Walburger, Vincent Fourmond
Summary: Metal-based formate dehydrogenases are enzymes that require molybdenum or tungsten ions to catalyze the conversion between formate and CO2. The coordination of the metal ion in the active form prevents direct binding of formate to the metal. The study's findings provide strong evidence for the hypothesis that the oxidation of formate occurs in the second coordination sphere of the metal.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2023)
Article
Microbiology
Delfim Ferreira, Sofia S. S. Venceslau, Raquel Bernardino, Andre Preto, Lichun Zhang, Jacob R. R. Waldbauer, William D. D. Leavitt, Ines A. C. Pereira
Summary: DsrC is a crucial protein in dissimilatory sulfur metabolism, serving as a co-substrate of the dissimilatory sulfite reductase DsrAB. It has been found to have additional functions beyond sulfite reduction. In this study, the role of DsrC in fermentative growth of Desulfovibrio vulgaris Hildenborough was investigated, and it was found that impairment of DsrC function led to reduced growth and a shift towards more fermentative metabolism.
ENVIRONMENTAL MICROBIOLOGY
(2023)
Article
Biochemistry & Molecular Biology
Guilherme Vilela-Alves, Rita Rebelo Manuel, Ana Rita Oliveira, Ines Cardoso Pereira, Maria Joao Romao, Cristiano Mota
Summary: In this study, the Desulfovibrio vulgaris Hildenborough SeCys/W-Fdh was characterized by time-resolved X-ray crystallography, revealing intermediate structures and changes during formate oxidation. Formate molecules were identified in the catalytic pocket of the Fdh for the first time. Moreover, the redox reversibility of DvFdhAB in crystals was confirmed.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Chemistry, Multidisciplinary
Vladimir Pelmenschikov, Delfim Ferreira, Sofia S. Venceslau, Peter Hildebrandt, Ines A. . C. Pereira, Smilja Todorovic, Smilja Todorovic
Summary: In this study, resonance Raman spectroscopy and density functional theory calculations were used to investigate the structural, electronic, and vibrational properties of the noncubane [4Fe-4S] cluster in heterodisulfide reductase (HdrB). Homology modeling was employed to predict the protein environment of the neighboring clusters in DvHdrB. The results showed that the oxidized [4Fe-4S](3+) cluster adopts a closed conformation in the absence of substrate, but transitions to an open structure upon substrate coordination, accompanied by a ligand switch. This study provides valuable insights for future research on enzymes with this unconventional cofactor.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Article
Chemistry, Physical
Andreas Rutz, Chandan K. Das, Andrea Fasano, Jan Jaenecke, Shanika Yadav, Ulf-Peter Apfel, Vera Engelbrecht, Vincent Fourmond, Christophe Leger, Lars Schaefer, Thomas Happe
Summary: The active site of [FeFe]-hydrogenases degrades upon contact with oxygen, but the protein structure of a certain hydrogenase (CbA5H) allows its active site to be protected, reducing degradation caused by oxygen. By modifying the surface residue, the hydrogenase's resistance to oxygen can be increased.
Article
Chemistry, Multidisciplinary
Samuel J. Cobb, Azim M. Dharani, Ana Rita Oliveira, Ines A. C. Pereira, Erwin Reisner
Summary: The electrolysis of dilute CO2 streams is hampered by low concentrations of dissolved substrate and rapid depletion at the electrolyte-electrocatalyst interface. To address this issue, a bio-inspired strategy mimicking the carboxysome in cyanobacteria is introduced. It utilizes microcompartments with nanoconfined enzymes in a porous electrode to accelerate CO2 hydration kinetics and minimize substrate depletion, enabling efficient reduction of low-concentration CO2 to formate even at atmospheric concentrations. This concept demonstrates the potential of the carboxysome as a blueprint for the reduction of low-concentration CO2 streams to chemicals.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2023)
Article
Chemistry, Inorganic & Nuclear
Cheriehan Hessin, Jules Schleinitz, Nolwenn Le Breton, Sylvie Choua, Laurence Grimaud, Vincent Fourmond, Marine Desage-El Murr, Christophe Leger
Summary: Potential inversion refers to the phenomenon where the second electron transfer is easier than the first, and it is significant for understanding enzyme catalysis and developing efficient catalysts. Currently, there is a lack of analytical predictions to interpret voltammetric peak potentials when potential inversion occurs, and cyclic voltammograms are often analyzed without considering overfitting or estimating error. In this study, a theory for voltammetry of two-electron redox species in the irreversible limit is formulated and applied to analyze the voltammetry of a nickel complex with redox-active ligands, highlighting the intrinsic underdetermination of the model. Characterizing the thermodynamics of two-electron electron-transfer reactions is crucial for catalyst design.
INORGANIC CHEMISTRY
(2023)
Correction
Chemistry, Multidisciplinary
Vincent Fourmond, Carole Baffert, Kateryna Sybirna, Thomas Lautier, Abbas Abou Hamdan, Sebastien Dementin, Philippe Soucaille, Isabelle Meynial-Salles, Herve Bottin, Christophe Leger
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Article
Ecology
Sinje Neukirchen, Ines A. C. Pereira, Filipa L. Sousa
Summary: Microbial dissimilatory sulfur metabolism plays a significant role in Earth's biochemical sulfur cycle. Comparative genomics and phylogenetic analyses indicate an archaeal origin of the minimal DsrABCMK(N) protein set, with sulfite reduction as its primordial function. The acquisition of additional Dsr proteins increased the complexity of the Dsr pathway. Further discoveries of two types of Qmo complexes allowed microorganisms to use sulfate as an electron acceptor. Chlorobi and Proteobacteria evolved the ability to use the Dsr pathway for sulfur oxidation independently.
Article
Chemistry, Multidisciplinary
Andrea Fasano, Chloe Guendon, Aurore Jacq-Bailly, Arlette Kpebe, Jeremy Wozniak, Carole Baffert, Melisa del Barrio, Vincent Fourmond, Myriam Brugna, Christophe Leger
Summary: The observation that some homologous enzymes have the same active site but very different catalytic properties demonstrates the importance of long-range effects in enzyme catalysis. In this study, the catalytic bias and sensitivity of hydrogenase 1 (Hyd 1) were found to be determined by the catalytic subunit rather than the electron transfer chain, and the proximal cluster was confirmed to play a role in the enzyme's resistance to long-term exposure to O-2. This research provides insights into the structure-function relationships of hydrogenases and offers possibilities for engineering useful hydrogenases with desired properties.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Correction
Chemistry, Multidisciplinary
Vincent Fourmond, Carole Baffert, Kateryna Sybirna, Thomas Lautier, Abbas Abou Hamdan, Philippe Soucaille, Isabelle Meynial-Salles, Christophe Leger
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
