Formate dehydrogenases bacteria

Formamidine, N,N -di-2-anthraquinonyI-metal complexes, 2,275 Formamidine, IV.AT-diaryl-metal complexes, 2, 275 Formamidine, N, N -dibenzyl-metal complexes, 2,276 Formamidine, IV.N -diisopropyl-metal complexes, 2, 276 Formamidinesulfinic acid technetium complexes, 6, 974 Formate dehydrogenases bacteria... 

Formate dehydrogenase Bacteria - E. coli 600 a2fhY2 4 Heme b... 

Fluorites inclusions, 869 Formaldehyde hydroformylation catalysts, rhodium complexes, 261 Forraamidinesulfinic acid technetium complexes, 974 Formate dehydrogenases bacteria... 

In two sulfate-reducing bacteria we found oxygen-tolerant formate dehydrogenases with different subunit composition. The formate dehydrogenase from D. desulfuricans is an af3y protein whereas the one from D. gigas is an afi protein. Both proteins contain two MGD cofactors but the protein from D. desulfuricans contains four heme c attached to the y subunit (16 kDa). 

The second E. coli example also involves contextual signals that alter coding patterns. A few proteins in all cells (such as formate dehydrogenase in bacteria and glutathione peroxidase in mammals) require the element selenium for their activity, generally in the form of the modified amino acid selenocysteine. Although modified amino acids are generally produced in posttranslational reactions (described in Section... 

Several selenoproteins have been found in certain bacteria and archaea. A hydrogenase from Methano-coccus vannielii contains selenocysteine.559 560 This enzyme transfers electrons from H2 to the C-5 si face of the 8-hydroxy-5-deazaflavin cofactor F q (Section B,4). The same bacterium synthesizes two formate dehydrogenases (see Fig 15-23), one of which contains Se. Two Se-containing formate dehydrogenases are made by E. coli. One of them, which is coupled to a hydrogenase in the formate hydrogen-lyase system (see Eq. 15-37), is a 715-residue protein containing selenocysteine at position 140.561-563 The second has selenocysteine at position 196 and functions with a nitrate reductase in anaerobic nitrate respiration.561... 

A number of other reductases and dehydrogenases, including dissimilatory nitrate reductases of E. coli and of denitrifying bacteria (Chapter 18), belong to the DMSO reductase family. Other members are reductases for biotin S-oxide,649 trimethylamine N-oxide, and polysulfides as well as formate dehydrogenases (Eq. 16-63), formylmethanofuran dehydrogenase (Fig. 15-22,... 

Formate dehydrogenases from many bacteria contain molybdopterin and also often selenium (Table 15-4).664/665 A membrane-bound Mo-containing formate dehydrogenase is produced by E. coli grown anaerobically in the presence of nitrate. Under these circumstances it is coupled to nitrate reductase via an electron-transport chain in the membranes which permits oxidation of formate by nitrate (Eq. 18-26). This enzyme is also a multisubunit protein.665 666 Two other Mo- and Se- containing formate dehydrogenases are produced... 

In bacteria, which lack formate dehydrogenase, formaldehyde can be oxidized to C02 to provide energy beginning with the reactions of Eq. 17-51. The resulting fructose 6-P is isomerized to glucose 6-P, which is then dehydrogenated via Eq. 17-12 to form C02 and the regenerating substrate ribulose 5-phosphate. 

Formate dehydrogenases have been isolated from aerobic and anaerobic bacteria, yeasts and plants, and comprise a rather heterogeneous group of enzymes. E. coli contains two forms of formate dehydrogenase which can be either soluble or membrane bound.1040... 

Formate dehydrogenases occur in anaerobic bacteria (20) and catalyze the oxidation of formate to carbon dioxide. 

Enzymes in this family include DMSO reductase, biotin 5-oxide reductase, dissimilatory nitrate reductase, trimethylamine A-oxide reductase, and formate dehydrogenase they are found exclusively in bacteria and fungi and act as terminal respiratory reductases during anaerobic growth in the presence of their respective substrates. " DMSO reductases catalyze the reaction shown in equation (5) the water-soluble enzymes from the purple phototrophic bacteria R. capsula-tus and R. sphaeroides are among the simplest Mo-MPT enzymes, being relatively small (ca. 85 kDa), single subunit... 

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