By H. W. Doelle
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This reduced NAD can no longer form a complex with enzyme I and is released. The NADH + H + can then complex with an enzyme II at some other stage in a metabolic pathway and in this complex can reduce another substrate, itself being reoxidized to NAD+ and again released, thus returning to the cycle (Fig. 6). NAD+ therefore forms a link between two enzymes. The production of NADH + H + during a reaction causes a rise in the spectrophotometer absorption band at 340 nm. OH I O \ OH Fig. 5. Nicotinamide-adenine dinucleotide phosphate (NADP).
The reaction should never be written NAD -> NADH 2 . The same rules apply for NADP. The pyridine ring in the coenzyme is attached in iV-glycosidic linkage to ribose. This linkage is possible only with the pyridinium cation, which bears one hydrogen atom on the nitrogen (Fig. 4). Pyrophosphoric acid provides the linkage between nicotinamide riboside and adenosine. In nicotinamide-adenine dinucleotide phosphate the adenosine moiety carries the additional phosphate group in the 2' position (see Fig.
3 Some Electrode Potentials of Biological Interest*1 EQ Couple 2 H 2 0 ^± 0 2 + 4 H + + 4 e N0 2 - + H 2 0 ^± NO3- + 2 H + + 2 e H202 ^ 0 2 + 2 H + + 2 e Cyt. a32+ ^ cyt. a33+ + 1 e Cyt. a2+ ;=± cyt. a3+ + 1 e Cyt. c2+ ^± cyt. c3+ + 1 e Succinate ^± fumarate + 2 H + + 2 e H 2 ^ 2 H + + 2e (pHO) Cyt. b 2+ ^± cyt. 699 From Dolin (4). , lactate) are electromotively passive. , lactate-pyruvate) estab lishes the potential of the lower end of the electron transport chain. , pyruvate) may enter a metabolic system while the released electrons proceed independently along the transport system.