NADH nicotinamide adenine

LHRH luteinizing hormone-releasing hormone NADH nicotinamide adenine dinucleotide, reduced form... 

Nicotinamide adenine dinucleotide (NADH), 24 348. See also NADH Nicotinamide adenine dinucleotide... 

Abbreviations NADH, nicotinamide-adenine dinucleotide phosphate TNS, 2-(p-toluidino)naphthalene-6-sulfonic acid. 

NADH nicotinamide-adenine dinucleotide Ru5P ribulose-5-phosphate... 

NADH Nicotinamide adenine dinucleotide. A molecule that carries energy. 

NADH nicotinamide adenine dinucleotide snRNP small nuclear ribonucleoprotein... 

In contrast to plant cells, which normally get their cellular energy from photosynthesis, animal cells need a carbohydrate source, usually glucose, and the amino acid glutamine. The catabolism of these substrates allows the production of two coenzymes (ATP and NADH - nicotinamide adenine dinucleotide), which are essential for maintaining the viability of the cells. These coenzymes can be used for the maintenance, metabolism and/or for the synthesis of particular desired products (Wagner, 1997). 

Figure 8-3. The components of oxidative phosphorylation located in the inner membrane of the mitochondria. ADP, adenosine diphosphate ATP, adenosine triphosphate NADH, nicotinamide adenine dinucleotide.

Enzymatic cofactors, such as nicotinamide adenine dinucleotide (NADH), nicotinamide adenine dinucleotide phosphate (NADPH), flavin adenine dinucleotide (EAD), flavin mononucleotide (EMN), and pyridoxal phosphate, are fluorescent and commonly found associated with various proteins where they are responsible for electron transport (see Fig. lb and Table 1). NADH and NADPH in the oxidized form are nonfluorescent, whereas conversely the flavins, FAD and EMN, are fluorescent only in the oxidized form. Both NADH and FAD fluorescence is quenched by the adenine found within their cofactor structures, whereas NADH-based cofactors generally remain fluorescent when interacting with protein structures. The fluorescence of these cofactors is often used to study the cofactors interaction with proteins as well as with related enzymatic kinetics (1, 9-12). However, their complex fluorescent characteristics have not led to widespread applications beyond their own intrinsic function. 

Fig. 2.1. Examples from The Energy Hall of Fame. These molecules not only deliver energy, but transfer special groups in the process. Acyl, RCO— ADP, adenosine diphosphate ATP, adenosine triphosphate dUMP deoxyuridine monophosphate FAD, flavin adenine dinucleotide GTP, guanosine triphosphate NADH, nicotinamide adenine dinucleotide NADP, nicotinamide adenine dinucleotide phosphate P, phosphate TMP, thymidine monophosphate UDP, uridine diphosphate UTP, uridine triphosphate.

NADH nicotinamide-adenine dinucleotide reduced form... 

The second is the direct production pathway characteristic of the acetone-butanol fermentation by bacteria such as Clostridium butyricum. In this pathway, hydrogen is produced directly without formate production. This pathway, however, may be unified with NADH pathway, because the mass balance of NADH (Nicotinamide Adenine Dinucleotide, reduced form) shows the same result with NADH pathway. 

NADH (nicotinamide adenine dinucleotide) is a biochemical source of hydride. In the following example NADH reduces acetaldehyde to ethanol via minor pathway H t., hydride transfer to a cationic center. A Zn ion acts as a Lewis acid to polarize the acetaldehyde carbonyl (similar to protonating the carbonyl). The Lewis acid makes the carbonyl a better electron sink by increasing the partial positive charge on carbon. In fact, the electrophilic catalysis by 2+ and 3+ metal ions can accelerate additions to carbonyls by over a million times. The formation of the aromatic pyridinium ring in the NAD" product helps balance the energetics of this easily reversible reaction. 

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