NADH dehydrogenases

Preparations of NADH dehydrogenase from mammalian mitochondria may be divided into three types (1) NADH-ubiquinone reductase or complex I of the electron transport system, (2) the high molecular weight NADH dehydrogenases, and (3) the low molecular weight NADH dehy- 

Singer, in Non-Heme Iron Proteins (A. San Pietro, ed.), p. 349. Antioch Press, Yellow Springs, Ohio, 1965. 

Singer and M. Gutman, in Pyridine Nucleotide-Dependent Dehydrogenases (H. Sund, ed.), p. 375. Springer-Yerlag, Berlin and New York, 1970. 

Singer, in Biochemical Evolution and the Origin of Life (E. Schoffe-niels, ed.), p. 203. North-Holland Publ., Amsterdam, 1971. 

Singer, M. Gutman, and V. Massey, in Iron-Sulfur Proteins (W. Loven-berg, ed.), Vol. 1, p. 225. Academic Press, New York, 1973. 

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Hydroxyriboflavin. This compound [86120-61 -8] (26) was isolated as a green coen2yme of the NADH dehydrogenase from Peptostreptococms elsdenii and also from glycolate oxidase of porcine Hver. It is not fluorescent, and its stmcture was estabflshed by synthesis (106). The 5 -monophosphate serves as a cofactor for glycolate oxidase from pig Hver. 

Oxidation of P-nicotinamide adenine dinucleotide (NADH) to NAD+ has attracted much interest from the viewpoint of its role in biosensors reactions. It has been reported that several quinone derivatives and polymerized redox dyes, such as phenoxazine and phenothiazine derivatives, possess catalytic activities for the oxidation of NADH and have been used for dehydrogenase biosensors development [1, 2]. Flavins (contain in chemical structure isoalloxazine ring) are the prosthetic groups responsible for NAD+/NADH conversion in the active sites of some dehydrogenase enzymes. Upon the electropolymerization of flavin derivatives, the effective catalysts of NAD+/NADH regeneration, which mimic the NADH-dehydrogenase activity, would be synthesized [3]. 

As its name implies, this complex transfers a pair of electrons from NADH to coenzyme Q a small, hydrophobic, yellow compound. Another common name for this enzyme complex is NADH dehydrogenase. The complex (with an estimated mass of 850 kD) involves more than 30 polypeptide chains, one molecule of flavin mononucleotide (FMN), and as many as seven Fe-S clusters, together containing a total of 20 to 26 iron atoms (Table 21.2). By virtue of its dependence on FMN, NADH-UQ reductase is a jlavoprotein. 

The reduced NADH of the tespitatoty chain is in turn oxidized by a metalloflavoptotein enzyme—NADH dehydrogenase. This enzyme contains FeS and FMN, is tighdy bound to the tespitatoty chain, and passes te-ducing equivalents on to Q. 

NADH dehydrogenase Azotobacier vinelandii NADHb) Menadione... 

Bowles, J. and McManus, D.P. (1993b) NADH dehydrogenase 1 gene sequences compared for species and strains of the genus Echinococcus. InternationalJournal... 

The hydrobromide of ( )-6-chloro-5-(2-thienylvinyl)-2,3-dihydro-imidazo[2,l- ]thiazole 127 was found to be potent as an inhibitor of mitochondrial NADH dehydrogenase becoming a preferred target of commercial pesticides, especially insecticides and acaricides <1995JME1090, 1999EJM883>. 

AIFKGXVSNNLXXFP NADH dehydrogenase subunit F/172-20l/(Helianthostylis spruce i/53% 0.2... 

NADH is oxidized by NADH dehydrogenase (complex I), delivering its electrons into the chain and returning as NAD to enzymes that require it. The electrons are passed along a series of protein and lipid carriers that serve as the wire. These include, in order ... 

NADH dehydrogenase (complex I) accepts electrons from NADH... 

NADH dehydrogenase (ubiquinone) [FAD, Fe2S2, Fe4S4]— complex 1 ... 

NADH dehydrogenase (ubiquinone) [EC 1.6.5.3] (also called ubiquinone reductase, type I dehydrogenase, and complex I dehydrogenase) catalyzes the reaction of NADH with ubiquinone to produce NAD and ubiqui-nol. The complex, which uses EAD and iron-sulfur proteins as cofactors, is found in mitochondrial membranes and can be degraded to form NADH dehydrogenase [EC... 

I. 6.99.3]. NADH dehydrogenase [EC 1.6.99.3] catalyzes the reaction of NADH with an acceptor to produce NAD+ and the reduced acceptor. Iron-sulfur and flavo-proteins are still being used as cofactors with this component of EC 1.6.5.3. Interestingly, after certain preparations have been followed, cytochrome c may serve as the acceptor substrate. 

CYTOCHROME cj HYDROGENASE CYTOCHROME c PEROXIDASE CYTOCHROME P-450 REDUCTASE MIXED-EUNCTION OXIDASE NADH-CYTOCHROME bs REDUCTASE NADH DEHYDROGENASE NITRATE REDUCTASE... 

IMIDAZOLEACETATE HYDROXYLASE NADH-CYTOCHROME bs REDUCTASE NADH DEHYDROGENASE... 

NADH PEROXIDASE NITRATE REDUCTASE NADH-CYTOCHROME bj REDUCTASE NADH DEHYDROGENASE NADH DEHYDROGENASE (Other Than Complex I)... 

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