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In recent years, CO2 reduction and utilization have been proposed as an innovative solution for global warming and the ever-growing energy and raw material demands. In contrast to various classical methods, including chemical, electrochemical, and photochemical methods, enzymatic methods offer a green and sustainable option for CO2 conversion. In addition, enzymatic hydrogenation of CO2 into platform chemicals could be used to produce economically useful hydrogen storage materials, making it a win-win strategy. The thermodynamic and kinetic stability of the CO2 molecule makes its utilization a challenging task. However, Nicotine adenine dinucleotide (NAD+)-dependent formate dehydrogenases (FDHs), which have high selectivity and specificity, are attractive catalysts to overcome this issue and convert CO2 into fuels and renewable chemicals. It is necessary to improve the stability, cofactor necessity, and CO2 conversion efficiency of these enzymes, such as by combining them with appropriate hybrid systems. However, metal-independent, NAD+-dependent FDHs, and their CO2 reduction activity have received limited attention to date. This review outlines the CO2 reduction ability of these enzymes as well as their properties, reaction mechanisms, immobilization strategies, and integration with electrochemical and photochemical systems for the production of formic acid or formate. The biotechnological applications of FDH, future perspectives, barriers to CO2 reduction with FDH, and aspects that must be further developed are briefly summarized. We propose that constructing hybrid systems that include NAD+-dependent FDHs is a promising approach to convert CO2 and strengthen the sustainable carbon bio-economy. [ABSTRACT FROM AUTHOR]

NADPH-dependent oxidoreductases are crucial biocatalysts for the industrial production of chiral compounds. For in situ recycling of required expensive cofactors in this biosynthetic process, NAD(P)+-dependent formate dehydrogenases (FDHs) are wanted to be employed as redox biocatalysts due to their greener and process friendly nature. However, their utilization is limited by their undesired cofactor preference that strongly prone to NAD+ more than NADP+ and catalytic efficiency. To mine NADP+-dependent FDHs in nature by the guidance of bioinformatic tools or re-engineering of their NAD+-dependent equivalents to get an applicable recycler are attractive topics in bioengineering. It can be said that, up to now, the attempts to switch the cofactor preference of the FDHs generally have resulted in NADP+-dependent enzymes that have not to catch the desired catalytic efficiencies or stability. In this review, all studies about the native NADP+-dependent FDHs and also engineered equivalents that reconstructed with different protein engineering approaches for altering the coenzyme specificity are outlined. To switch the coenzyme preference of FDHs or to find the native NADP+-dependent FDHs will be the hot topics in bioengineering until finding a feasible regenerator. Therefore, this study will be a useful guide to get a pathway for designing or discovering novel NADP+-dependent FDHs. [ABSTRACT FROM AUTHOR]

NAD+-dependent formate dehydrogenases (FDHs, E.C 1.2.1.2) catalyse the reversible reaction of CO2 to formate ion (HCOO−) and reduces NAD+ molecule to NADH. Previously described FDHs from Chaetomium thermophilum (CtFDH) and Ceriporiopsis subvermispora (CsFDH) are active against formate and HCO3–. In this study, we examined the functional effects of active site mutations in Ct and Cs NAD+-dependent FDHs. The residues Ile94, Asn120, Val310, His312 at CtFDH and Asn312, Val313, Val331 at CsFDH are located in the active site. The effects of amino acid changes on catalytic properties and thermal stability of CtFDH and CsFDH revealed some interesting results compared with structurally equivalent positions that have been studied in the literature. The strongest effect was observed in CsFDH Val313Pro against HCO3–. The KM value of the CsFDH Val313 enzyme for HCO3– substrate dramatically decreased, and enzyme activity increased. In CtFDH mutants, all enzymes except Val310Asn showed an increased kcat value when KM values increase. Analyses of results of mutant CtFDHs and CsFDHs give some promising results for CO2 reduction as compared to the literature. Structural analyses of the substrate-binding site were done by homology modelling. [ABSTRACT FROM AUTHOR]

The accumulation of carbon dioxide in the atmosphere as a result of human activities has caused a number of adverse circumstances in the world. For this reason, the proposed solutions lie within the aim of reducing carbon dioxide emissions have been quite valuable. However, as the human activity continues to increase on this planet, the possibility of reducing carbon dioxide emissions decreases with the use of conventional methods. The emergence of compounds than can be used in different fields by converting the released carbon dioxide into different chemicals will construct a fundamental solution to the problem. Although electro-catalysis or photolithography methods have emerged for this purpose, they have not been able to achieve successful results. Alternatively, another proposed solution are enzyme based systems. Among the enzyme-based systems, pyruvate decarboxylase, carbonic anhydrase and dehydrogenases have been the most studied enzymes. Pyruvate dehydrogenase and carbonic anhydrase have either been an expensive method or were incapable of producing the desired result due to the reaction cascade they catalyze. However, the studies reporting the production of industrial chemicals from carbon dioxide using dehydrogenases and in particular, the formate dehydrogenase enzyme, have been remarkable. Moreover, reported studies have shown the existence of more active and stable enzymes, especially the dehydrogenase family that can be identified from the biome. In addition to this, their redesign through protein engineering can have an immense contribution to the increased use of enzyme-based methods in CO2 reduction, resulting in an enormous expansion of the industrial capacity. [ABSTRACT FROM AUTHOR]