Journal of Molecular Biology
Regular ArticleHigh Resolution Structures of Holo and Apo Formate Dehydrogenase
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Chimeric versus isolated proteins: Biochemical characterization of the NADP<sup>+</sup>-dependent formate dehydrogenase from Pseudomonas sp. 101 fused with the Baeyer-Villiger monooxygenase from Thermobifida fusca
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2022, Molecular CatalysisCitation Excerpt :Then the active center is closed to avoid interference of the surrounding solvent water molecules on the hydride transfer. In the ternary complex, the hydride is transferred directly from the C4N atom of the NAD+ to generate NADH, and this transfer process seems to be the only rate-limiting step in the catalytic mechanism of FDH [6, 7]. FDH is widely used for cofactor regeneration instead of adding coenzyme directly to control the cost in the processes of chiral synthesis with NAD(P)+-dependent oxidoreductases [8].
The role of Tyr102 residue in the functioning of bacterial NAD<sup>+</sup>-dependent formate dehydrogenase of Pseudomonas sp. 101
2022, Biochemical and Biophysical Research CommunicationsCitation Excerpt :It was previously suggested that the binding of both the co-enzyme and substrate leads to the transition from the open to the closed conformation [2]. This suggestion was based on the analysis of two 3D-structures of PseFDH: an apo-form (PDB: 2NAC) and a holo-form (PDB: 2NAD, which is a triple complex of PseFDH, NAD+, and the azide ion) [2]. It was found that the transition from apo- to holo-enzyme is associated with the narrowing of the outer neck of the PseFDH substrate channel, due to the movement of catalytic domains relative to co-enzyme binding domains [3].
Structural insights into the NAD<sup>+</sup>-dependent formate dehydrogenase mechanism revealed from the NADH complex and the formate NAD<sup>+</sup> ternary complex of the Chaetomium thermophilum enzyme
2020, Journal of Structural BiologyCitation Excerpt :The formate molecule in the active site is kept in place by H-bonds to the main chain nitrogen of Ile94 and the side chain of Asn120 on one side and the side chains of Arg259 and His312 on the other side (Fig. 5; Figure S3). The formate molecule is bound to the CtFDH catalytic site in a position close to the site of the azide molecule binding in the ternary NAD+ azide complexes in structures of FDHs from other sources (Lamzin et al., 1994; Fig. 6a). The formate molecule binds to the apo structure of the Pseudomonas FDH in approximately the same place and orientation (Filippova et al., 2006; Fig. 6b).