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NAD reductase

NITRITE REDUCTASE NITROGENASE PYRUVATE SYNTHASE RUBREDOXIN NAD REDUCTASE STEROID 11 -HYDROXYLASE SULFITE REDUCTASE TUNGSTOENZYMES... [Pg.742]

RUBREDOXIN.NAD REDUCTASE SUCCINATE DEHYDROGENASE SULFITE REDUCTASE SULFUR DIOXYGENASE THYMIDINE 2 -HYDROXYLASE XANTHINE OXIDASE Iron(ll) hydroxide (Fe(OH)2),... [Pg.752]

RUBREDOXIN NAD REDUCTASE SERINE DEHYDROGENASE SORBITOL DEHYDROGENASE XANTHINE DEHYDROGENASE NAD formation,... [Pg.764]

However, in contrast to the cyclic flow of electrons in purple bacteria, some electrons flow from the reaction center to an iron-sulfur protein, ferredoxin, which then passes electrons via ferredoxin NAD reductase to NAD+, producing NADH. The electrons taken from the reaction center to reduce NAD+ are replaced by the oxidation of H2S to elemental S, then to SOf, in the reaction that defines the green sulfur bacteria. This oxidation of H2S by bacteria is chemically analogous to the oxidation of H20 by oxygenic plants. [Pg.732]

This enzyme is homologous to the ferredoxin NAD reductase of green sulfur bacteria (Fig. 19-47b). [Pg.734]

Bes T, Gomez-Moreno C, Guisan JM et al. (1995) Selective enzymatic oxidations stabiUzation by multipoint covalent attachment of ferredoxin NAD-reductase an interesting cofactor recycling enzyme. J Mol Catal 98 161-169... [Pg.197]

NADH-cytochrome reductase NADH NAD + FAD Fe respira-tory chain cytochrome b ... [Pg.79]

The NAD- and NADP-dependent dehydrogenases catalyze at least six different types of reactions simple hydride transfer, deamination of an amino acid to form an a-keto acid, oxidation of /3-hydroxy acids followed by decarboxylation of the /3-keto acid intermediate, oxidation of aldehydes, reduction of isolated double bonds, and the oxidation of carbon-nitrogen bonds (as with dihydrofolate reductase). [Pg.590]

Sequences of proteins containing Rieske-type clusters have been deduced from the complete operons of several dioxygenases these dioxygenases require electrons from NAD(P)H to convert aromatic compounds to cis-arene diols. The water-soluble dioxygenase systems consist of a reductase and a terminal dioxygenase many dioxygenases also contain a [2Fe-2S] ferredoxin (20). The terminal oxygenases contain a Rieske-type cluster and the ferredoxins may contain either a Rieske-type or a 4-cysteine coordinated [2Fe-2S] cluster. [Pg.89]

The dioxygenase systems consist of a reductase and a terminal oxygenase many dioxygenases also contain a [2Fe-2S] ferredoxin. The reductase reacts with NAD(P)H it can be any of the following (20) ... [Pg.149]

Figure 22-4. Sequence of reactions in the oxidation of unsaturated fatty acids, eg, linoleic acid. A -c/s-fatty acids or fatty acids forming A -c/s-enoyl-CoA enter the pathway at the position shown. NADPH for the dienoyl-CoA reductase step is supplied by intramitochondrial sources such as glutamate dehydrogenase, isocitrate dehydrogenase,and NAD(P)H transhydrogenase. Figure 22-4. Sequence of reactions in the oxidation of unsaturated fatty acids, eg, linoleic acid. A -c/s-fatty acids or fatty acids forming A -c/s-enoyl-CoA enter the pathway at the position shown. NADPH for the dienoyl-CoA reductase step is supplied by intramitochondrial sources such as glutamate dehydrogenase, isocitrate dehydrogenase,and NAD(P)H transhydrogenase.
Dimeric flavoprotein chromate reductases have been purified from Pseudomonas putida (ChrR) and Escherichia coli (YieF). The former produces a semiquinone and transiently reactive oxygen species, whereas the latter is an obligate four-electron reductant. One-electron reduction of Cr(Vl) to Cr(V) has, however, been observed as an intermediate in the reduction by the NAD(P)H-dependent reductase of Pseudomonas ambigua strain G-1 (Suzuki et al. 1992). [Pg.165]

Rohde BH, R Schmid, MS Ullrich (1999) Thermoregulated expression and characterization of an NAD(P)H-dependent 2-cyclohexen-l-one reductase in the plant pathogenic bacterium Pseudomonas syringae pv. glycineti J Bacteriol 181 814-822. [Pg.167]

Metabolism of trimethylamine oxide in fish muscle involves an enzyme-catalyzed oxidation-reduction reaction. The enzyme responsible for the conversion of trimethylamine oxide to trimethylamine is known as trimethylamine-W-oxide reductase. This enzyme acts on nicotinamide adenine dinucleotide (NADH) and TMAO to produce NAD+, trimethylamine and water (Fig. 13.13.1). TMAO acts as the oxidizing agent and is reduced, while NADH undergoes oxidation as the reducing agent. [Pg.194]

There is some evidence that the iron-sulfur protein, FhuF, participates in the mobilization of iron from hydroxamate siderophores in E. coli (Muller et ah, 1998 Hantke, K. unpublished observations). However, a reductase activity of FhuF has not been demonstrated. Many siderophore-iron reductases have been shown to be active in vitro and some have been purified. The characterization of these reductases has revealed them to be flavin reductases which obtain the electrons for flavin reduction from NAD(P)H, and whose main functions are in areas other than reduction of ferric iron (e.g. flavin reductase Fre, sulfite reductase). To date, no specialized siderophore-iron reductases have been identified. It has been suggested that the reduced flavins from flavin oxidoreductases are the electron donors for ferric iron reduction (Fontecave et ah, 1994). Recently it has been shown, after a fruitless search for a reducing enzyme, that reduction of Co3+ in cobalamin is achieved by reduced flavin. Also in this case it was suggested that cobalamins and corrinoids are reduced in vivo by flavins which may be generated by the flavin... [Pg.106]


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See also in sourсe #XX -- [ Pg.43 ]




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Ferredoxin-NAD reductase

NAD+

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