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The main reasons for the common use of enzymes in biosensors are: 1) ability to catalyze a large number of reactions; 2) potential to detect a group of analytes (substrates, products, inhibitors, and modulators of the catalytic activity); and 3) suitability with several different transduction methods for detecting the analyte.
d -Glucose + 2 [NAD] + + 2 [ADP] + 2 [P] i 2 × Pyruvate 2 × + 2 [NADH] + 2 H + + 2 [ATP] + 2 H 2 O Glycolysis pathway overview The use of symbols in this equation makes it appear unbalanced with respect to oxygen atoms, hydrogen atoms, and charges. Atom balance is maintained by the two phosphate (P i) groups: Each exists in the form of a hydrogen phosphate anion, dissociating to contribute ...
Members of this family include oxygen-insensitive NAD(P)H nitroreductase (flavin mononucleotide-dependent nitroreductase) (6,7-dihydropteridine reductase) (EC 1.5.1.34) and NADH dehydrogenase (EC 1.6.99.3). A number of these proteins are described as oxidoreductases.
In amperometric biosensors, an enzyme-catalyzed redox reaction causes a redox electron current that is measured by a working electrode. [11] Amperometric biosensors have been used in bio-MEMS for detection of glucose, galactose, lactose, urea, and cholesterol, as well as for applications in gas detection and DNA hybridization. [11]
Enzymatic reaction catalyzed by NDH-2. In yellow is represented the protein surface, sitting in the membrane (in gray) NDH-2, also known as type II NADH:quinone oxidoreductase or alternative NADH dehydrogenase, is an enzyme (EC: 1.6.99.3) which catalyzes the electron transfer from NADH (electron donor) to a quinone (electron acceptor), being part of the electron transport chain. [1]
Including one H + for the transport reactions, this means that synthesis of one ATP requires 1 + 10/3 = 4.33 protons in yeast and 1 + 8/3 = 3.67 in vertebrates. This would imply that in human mitochondria the 10 protons from oxidizing NADH would produce 2.72 ATP (instead of 2.5) and the 6 protons from oxidizing succinate or ubiquinol would ...
α-ketoglutarate + NAD + + CoA → Succinyl CoA + CO 2 + NADH Oxoglutarate dehydrogenase (α-Ketoglutarate dehydrogenase) This reaction proceeds in three steps: decarboxylation of α-ketoglutarate, reduction of NAD + to NADH, and subsequent transfer to CoA, which forms the end product, succinyl CoA. ΔG°' for this reaction is -7.2 kcal mol −1.
[3] Fig. 1. Schematic overview of fermentative and oxidative glucose metabolism of Saccharomyces cerevisiae. (A) upper part of glycolysis, which includes two sugar phosphorylation reactions. (B) fructose-1,6-bisphosphate aldolase, splitting the C6-molecule into two triose phosphates (C) triosephosphate isomerase, interconverting DHAP and GAP.