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1,2-Dihydronicotinamide adenine dinucleotide (NADH) is a vital coenzyme in cellular metabolism, playing a crucial role in redox reactions. It is the reduced form of nicotinamide adenine dinucleotide (NAD+), which is involved in various biological processes, including energy production, cellular respiration, and DNA repair. NADH is synthesized from NAD+ and an electron donor, typically through the action of dehydrogenase enzymes. It transfers electrons to other molecules, facilitating the conversion of nutrients into energy. The interconversion between NADH and NAD+ is essential for maintaining cellular redox balance and is a key component in the electron transport chain, which is central to ATP production.

2797-78-6

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2797-78-6 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 2797-78-6 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 2,7,9 and 7 respectively; the second part has 2 digits, 7 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 2797-78:
(6*2)+(5*7)+(4*9)+(3*7)+(2*7)+(1*8)=126
126 % 10 = 6
So 2797-78-6 is a valid CAS Registry Number.

2797-78-6Upstream product

2797-78-6Downstream Products

2797-78-6Relevant academic research and scientific papers

A genetically encodable ligand for transfer hydrogenation

Mayer, Clemens,Hilvert, Donald

, p. 3427 - 3431 (2013)

Simple tripeptides are shown here to be versatile ligands for iridium-catalyzed transfer hydrogenations affording large acceleration effects. A water-soluble iridium complex with Gly-Gly-Phe, for example, catalyzes the reduction of diverse ketones, aldehydes, and imines by formate with turnover frequencies rivaling or outperforming those of established ligand systems. Regioselective reduction of coenzyme NAD+ to NADH illustrates the potential utility of this system for biotechnological applications. Because peptides are genetically encodable, they represent an attractive class of foldamer ligands for creating artificial metalloenzymes.

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