Choe, Hyunjun Ha, Jung Min Joo, Jeong Chan Kim, Hyunook Yoon, Hye-Jin Kim, Seonghoon Son, Sang Hyeon Gengan, Robert M. Jeon, Seung Taeg Chang, Rakwoo Jung, Kwang Deog Kim, Yong Hwan Lee, Hyung Ho 2024-01-20T08:00:35Z 2024-01-20T08:00:35Z 2021-09-04 2015-02 2059-7983 https://pubs.kist.re.kr/handle/201004/125826 CO2 fixation is thought to be one of the key factors in mitigating global warming. Of the various methods for removing CO2, the NAD-dependent formate dehydrogenase from Candida boidinii (CbFDH) has been widely used in various biological CO2-reduction systems; however, practical applications of CbFDH have often been impeded owing to its low CO2-reducing activity. It has recently been demonstrated that the NAD-dependent formate dehydrogenase from Thiobacillus sp. KNK65MA (TsFDH) has a higher CO2-reducing activity compared with CbFDH. The crystal structure of TsFDH revealed that the biological unit in the asymmetric unit has two conformations, i.e. open (NAD(+)-unbound) and closed (NAD(+)-bound) forms. Three major differences are observed in the crystal structures of TsFDH and CbFDH. Firstly, hole 2 in TsFDH is blocked by helix alpha 20, whereas it is not blocked in CbFDH. Secondly, the sizes of holes 1 and 2 are larger in TsFDH than in CbFDH. Thirdly, Lys287 in TsFDH, which is crucial for the capture of formate and its subsequent delivery to the active site, is an alanine in CbFDH. A computational simulation suggested that the higher CO2-reducing activity of TsFDH is owing to its lower free-energy barrier to CO2 reduction than in CbFDH. English INT UNION CRYSTALLOGRAPHY HIGH-RESOLUTION STRUCTURES CARBON-DIOXIDE CO2 HYDROGENATION PURIFICATION SIMULATIONS REDUCTION MECHANISM PROTEINS ENERGY Structural insights into the efficient CO2-reducing activity of an NAD-dependent formate dehydrogenase from Thiobacillus sp KNK65MA Article 10.1107/S1399004714025474 1 Acta Crystallographica Section D - Structural Biology, v.71, pp.313 - 323 Acta Crystallographica Section D - Structural Biology 71 313 323 scie scopus 000349439900013 2-s2.0-84922594103 Biochemical Research Methods Biochemistry & Molecular Biology Biophysics Crystallography Biochemistry & Molecular Biology Biophysics Crystallography Article HIGH-RESOLUTION STRUCTURES CARBON-DIOXIDE CO2 HYDROGENATION PURIFICATION SIMULATIONS REDUCTION MECHANISM PROTEINS ENERGY CO2 reduction NAD-dependent formate dehydrogenase Thiobacillus sp. KNK65MA