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.
Development of an efficient and durable photocatalytic system for hydride reduction of an NAD(P)+ model compound using a ruthenium(II) complex based on mechanistic studies
Matsubara, Yasuo,Koga, Kichitaro,Kobayashi, Atsuo,Konno, Hideo,Sakamoto, Kazuhiko,Morimoto, Tatsuki,Ishitani, Osamu
, p. 10547 - 10552 (2010)
The mechanism of photocatalytic reduction of 1-benzylnicotinamidium cation (BNA+) to the 1,4-dihydro form (1,4-BNAH) using [Ru(tpy)(bpy)(L)] 2+ (Ru-L2+, where tpy = 2,2′:6′, 2′′-terpyridine, bpy = 2,2′-bipyridine, and L =
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.
Coupling Molecular Photocatalysis to Enzymatic Conversion
Mengele, Alexander K.,Seibold, Gerd M.,Eikmanns, Bernhard J.,Rau, Sven
, p. 4369 - 4376 (2017)
A hetero-binuclear dyad that contains a ruthenium polypyridyl moiety bound through an aromatic bridging ligand to an organometallic catalytic center has been used for the light-driven reduction of the N-benzyl-3-carbamoylpyridinium cation, NAD+
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
Precious-metal free photocatalytic production of an NADH analogue using cobalt diimine-dioxime catalysts under both aqueous and organic conditions
Au, Vonika Ka-Man,Cheng, Shun-Cheung,Ho, Pui-Yu,Ko, Chi-Chiu,Kwok, Chun-Leung,Leung, Chi-Fai,Man, Wai-Lun,Robert, Marc,Tsang, Po-Keung,Yiu, Shek-Man
, p. 7491 - 7494 (2020)
The photocatalytic generation of an NADH synthetic analogue, i.e. 1-benzyl-1,4-dihydronicotinamide (1,4-BNAH), has been studied using the cobalt diimino-dioxime complexes and the BF2-bridged derivative as catalysts. 1,4-BNAH was produced in both aqueous a
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.).
Transfer hydrogenations catalyzed by streptavidin-hosted secondary amine organocatalysts
Santi, Nicolò,Morrill, Louis C.,?widerek, Katarzyna,Moliner, Vicent,Luk, Louis Y. P.
supporting information, p. 1919 - 1922 (2021/03/02)
Here, the streptavidin-biotin technology was applied to enable organocatalytic transfer hydrogenation. By introducing a biotin-tethered pyrrolidine (1) to the tetrameric streptavidin (T-Sav), the resulting hybrid catalyst was able to mediate hydride transfer from dihydro-benzylnicotinamide (BNAH) to α,β-unsaturated aldehydes. Hydrogenation of cinnamaldehyde and some of its aryl-substituted analogues was found to be nearly quantitative. Kinetic measurements revealed that the T-Sav:1 assembly possesses enzyme-like behavior, whereas isotope effect analysis, performed by QM/MM simulations, illustrated that the step of hydride transfer is at least partially rate-limiting. These results have proven the concept thatT-Savcan be used to host secondary amine-catalyzed transfer hydrogenations.
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.
Biomimetic systems involving sequential redox reactions in glycolysis-the sulfur effect
Ogawa, Narihito,Furukawa, Sei,Kosugi, Yuya,Takazawa, Takayuki,Kanomata, Nobuhiro
, p. 12917 - 12920 (2020/11/05)
Magnesium hemithioacetates were used as model cysteine compounds to mimic natural hemithioacetals, and their biomimetic oxidation reactions using a model NAD+ compound were investigated. Cyclic hemithioacetate was found to be the best substrate for the reaction with the model NAD+ compound, which gave the corresponding NADH analog in excellent yield. This journal is
