Nicotinamide adenine dinucleotide molecular weight

Anaerobic azo dye reduction can be mediated by enzymes, low molecular weight redox mediators, and chemical reduction by biogenic reductants. These reactions can be located either intracellular or extracellular. Reduction of highly polar azo dyes, which cannot pass through the cell membranes, is located outside the cell. Like azo dyes, nicotinamide adenine dinucleotide phosphate, which is believed to be the main source of electrons, also cannot pass through the cell membranes. Azo reductase enzyme, which is oxygen-sensitive and released extracellularly, is found to be responsible for the reduction of azo dyes. 

Most of the electrons removed from fuels during energy metabolism are transferred via nicotinamide adenine dinucleotide (NAD). NAD collects electrons from many different energy fuels in reactions catalyzed by specific enzymes. These enzymes are dehydrogenases. Reduced NAD, in turn, shuttles the electrons to the respiratory chain. Flavin adenine dinucleotide (FAD) also acts as an electron shuttle. In each reaction involving NAD (or FAD), two electrons are transferred that is, two electrons are carried or shuttled. NAD and FAD are small molecules with molecular weights of 663 and 785 and are manufactured in the body from the vitamins niacin and riboflavin, respectively. These molecules are called N.A.D. and F.A.D., not nad" or Jad. ... 

Mediators can be polymerized on the electrode surface prior to enzyme immobilization, co-immobilized with enzyme, or simply added to the fuel solution. Common mediators used in BFC applications include low molecular weight, polymerizable, organic dyes such as methylene green, phenazines, and azure dyes, along with other redox-active compounds such as ferrocene, ferrocene derivalives, and conductive salts [14]. These mediators are often required for nicotinamide adenine dinucleotide (NAD )- and flavin adenine dinucleotide (FAD)-dependent enzymes, such as ADH, ALDH, and GOx. MET has been achieved at both cathodic and anodic interfaces through solution-phase mediators and mediators immobilized in various ways with or near the enzymes themselves [16,17]. However, these mediated systems do have drawbacks in that the species used to assist electron transfer are often not biocompatible, have short lifetimes themselves, or cause large potential losses. Table 5.1 lists common enzyme cofactors that can mediate or undergo DET with an enzyme on the electrode. 

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