952-92-1Relevant articles and documents
NAD(P) + -NAD(P)H MODEL - 43. FORMATION OF 1,4-DIHYDRONICOTINAMIDE IN THE REACTION OF PYRIDINIUM SALT AND GLYCERALDEHYDE.
Ohno,Ushida,Oka
, p. 1822 - 1825 (1983)
It has been found that N-substituted 1,4-dihydronicotinamides are produced by the reaction of N-substituted 3-carbamoylpyridinium salts with glyceraldehyde and its analogous compounds. A mechanism of the reaction is suggested.
NAD(P)+-NAD(P)H MODEL. REDUCTION OF PYRIDINIUM SALTS TO 1,4-DIHYDROPYRIDINES USING GLYCERALDEHYDE
Ohno, Atsuyoshi,Ushida, Satoshi,Oka, Shinzaburo
, p. 2487 - 2490 (1982)
N-Substituted 3-carbamoylpyridinium salts were reduced by glyceraldehyde to give 1,4-dihydronicotamide derivatives, which may be regarded as a model for oxidation by glyceraldehyde-3-phosphate dehydrogenase.
Unraveling the Light-Activated Reaction Mechanism in a Catalytically Competent Key Intermediate of a Multifunctional Molecular Catalyst for Artificial Photosynthesis
Dietzek, Benjamin,Gr?fe, Stefanie,Kupfer, Stephan,Mengele, Alexander Klaus,Pascher, Torbj?rn,Rau, Sven,W?chtler, Maria,Zedler, Linda,Zhang, Ying,Ziems, Karl Michael
, p. 13140 - 13148 (2019)
Understanding photodriven multielectron reaction pathways requires the identification and spectroscopic characterization of intermediates and their excited-state dynamics, which is very challenging due to their short lifetimes. To the best of our knowledg
Investigating the Structure-Reactivity Relationships Between Nicotinamide Coenzyme Biomimetics and Pentaerythritol Tetranitrate Reductase
Tan, Zhuotao,Han, Yaoying,Fu, Yaping,Zhang, Xiaowang,Xu, Mengjiao,Na, Qi,Zhuang, Wei,Qu, Xudong,Ying, Hanjie,Zhu, Chenjie
supporting information, p. 103 - 113 (2021/10/07)
Ene reductases (ERs) are attractive biocatalysts in terms of their high enantioselectivity and expanded substrate scope. Recent works have proved that synthetic nicotinamide coenzyme biomimetics (NCBs) can be used as easily accessible alternatives to natural cofactors in ER-catalyzed reactions. However, the structure-reactivity relationships between NCBs and ERs and influence factors are still poorly understood. In this study, a series of C-5 methyl modified NCBs were synthesized and tested in the PETNR-catalyzed asymmetric reductions. The physicochemical properties of these NCBs including electrochemical properties, stability, and kinetic behavior were studied in detail. The results showed that hydrophobic interaction caused by the introduced methyl group contributed to the stabilization of binding conformation in enzyme active site, resulting in comparable catalytic activity with that of NADPH. Molecular dynamics and steered molecular dynamics simulations were further performed to explain the binding mechanism between PETNR and NCBs, which revealed that stable catalytic conformation, appropriate donor-acceptor distance and angle, as well as free dissociation energy are important factors affecting the activity of NCBs. (Figure presented.).
Design of artificial metalloenzymes for the reduction of nicotinamide cofactors
Basle, Mattias,Padley, Henry A.W.,Martins, Floriane L.,Winkler, Gerlof Sebastiaan,J?ger, Christof M.,Pordea, Anca
, (2021/04/19)
Artificial metalloenzymes result from the insertion of a catalytically active metal complex into a biological scaffold, generally a protein devoid of other catalytic functionalities. As such, their design requires efforts to engineer substrate binding, in addition to accommodating the artificial catalyst. Here we constructed and characterised artificial metalloenzymes using alcohol dehydrogenase as starting point, an enzyme which has both a cofactor and a substrate binding pocket. A docking approach was used to determine suitable positions for catalyst anchoring to single cysteine mutants, leading to an artificial metalloenzyme capable to reduce both natural cofactors and the hydrophobic 1-benzylnicotinamide mimic. Kinetic studies revealed that the new construct displayed a Michaelis-Menten behaviour with the native nicotinamide cofactors, which were suggested by docking to bind at a surface exposed site, different compared to their native binding position. On the other hand, the kinetic and docking data suggested that a typical enzyme behaviour was not observed with the hydrophobic 1-benzylnicotinamide mimic, with which binding events were plausible both inside and outside the protein. This work demonstrates an extended substrate scope of the artificial metalloenzymes and provides information about the binding sites of the nicotinamide substrates, which can be exploited to further engineer artificial metalloenzymes for cofactor regeneration. Synopsis about graphical abstract: The manuscript provides information on the design of artificial metalloenzymes based on the bioconjugation of rhodium complexes to alcohol dehydrogenase, to improve their ability to reduce hydrophobic substrates. The graphical abstract presents different binding modes and results observed with native cofactors as substrates, compared to the hydrophobic benzylnicotinamide.
The visible-light-driven transfer hydrogenation of nicotinamide cofactors with a robust ruthenium complex photocatalyst
Chen, Fushan,Deng, Li,Dong, Wenjin,Tang, Jie,Xian, Mo,Zhao, Lijun
, p. 2279 - 2287 (2020/04/20)
The highly efficient regeneration of nicotinamide cofactors has been successfully achieved with a quantum yield (Φ) of 7.9 × 10-3via photocatalytic transfer hydrogenation in the presence of the ruthenium complex Ru(tpy)(biq)Cl2 (where tpy = 2,2′:6′,2′′-terpyridine and biq = 2,2′-bisquinoline). The photocatalytic system is not only highly efficient but also tolerant to amino acid residues. The combination of this photocatalyst with glutamate dehydrogenase enabled the controllable and efficient synthesis of l-glutamate to be realized. A mechanism involving light-induced ligand exchange, decarboxylation and hydride transfer has been proposed. Kinetic isotope experiments revealed that the decarboxylation of [Ru(tpy)(biq)HCOO]+ to [Ru(tpy)(biq)H]+ was the rate-determining step with a small apparent activation energy of 3.2 ± 0.4 kcal mol-1. The hydricity of [Ru(tpy)(biq)H]+ was estimated, via reaction equilibrium, to be 40 ± 3 kcal mol-1
