Sulfur reductase

Laska S, F Lottspeicht, A Kletzin (2003) Membrane-bound hydrogenase and sulfur reductase of the hyper-thermophilic and acidophilic archaeon AcidiawMi ambivalens. Microbiology (UK) 149 2357-2371. 

Ma, K., Schicho, R. N., Kelly, R. M. and Adams, M. W. W. (1993) Hydrogenase of the hyper-thermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase Evidence for a sulfur-reducing hydrogenase ancestor. Proc. Natl. Acad. Sci. USA, 90, 5341-4. 

Elemental sulfur was also formed during sulfide oxidation by a cytochrome c-flavocytochrome c-552 complex in Chromatium vinosum (42). Flavocytochromes of different phototrophic bacteria act as sulfide cytochrome c reductases and there was one report that a flavocytochrome possessed even elemental sulfur reductase activity (see 4.9V All flavocytochromes examined so far are heat-labile and are reduced by sulfide forming thiosulfate under strictly anaerobic conditions (4.9V The small acidic cytochromes c-551 of Ectothiorhodospira halochloris and Ectothiorhodospira abdelmalekii. both located on the outside of the cell membrane, stimulated the velocity of sulfide... 

Little is known about elemental sulfur reductase of the sulfur respiration system, though cytochrome c3 of the sulfate-reducing bacteria has been reported to reduce... 

A sulfur reductase has been obtained from a heterotroph, Wolinella succinogenes (Schroder et al., 1988). This sulfur reductase has molecular mass of 200 kDa (made up of 85 kDa subunits) and an Fe/S cluster, but no heme. The enzyme catalyzes the oxidation of formate with elemental sulfur in the presence of formate dehydrogenase. As formate dehydrogenase used here has cytochrome b, the sulfur-reducing system of the bacterium is said to include cytochrome b. 

The compositions of the described electron transport chains show participations of similar NiPe hydrogenases and similar polysulfide sulfur reductases in the case of W. succinogenes and A. ambivalens, whereas the sulfur reductase of P. abyss may be different. In this microorganism the electron transfer between the hydrogenases and the polysulfide sulfur reductases mediated by 8-methyl-menaquinone, sulfolobusquinone or cytochromes b and c, respectively, seems to be adapted to the synthesis capabilites of the species. 

A substantial fraction of the named enzymes are oxido-reductases, responsible for shuttling electrons along metabolic pathways that reduce carbon dioxide to sugar (in the case of plants), or reduce oxygen to water (in the case of mammals). The oxido-reductases that drive these processes involve a small set of redox active cofactors , that is, small chemical groups that gain or lose electrons. These cofactors include iron porjDhyrins, iron-sulfur clusters and copper complexes as well as organic species that are ET active. 

When induced in macrophages, iNOS produces large amounts of NO which represents a major cytotoxic principle of those cells. Due to its affinity to protein-bound iron, NO can inhibit a number of key enzymes that contain iron in their catalytic centers. These include ribonucleotide reductase (rate-limiting in DNA replication), iron-sulfur cluster-dependent enzymes (complex I and II) involved in mitochondrial electron transport and cis-aconitase in the citric acid cycle. In addition, higher concentrations of NO,... 

This key enzyme of the dissimilatory sulfate reduction was isolated from all Desulfovibrio strains studied until now 135), and from some sulfur oxidizing bacteria and thermophilic Archaea 136, 137). The enzymes isolated from sulfate-reducing bacteria contain two [4Fe-4S] clusters and a flavin group (FAD) as demonstrated by visible, EPR, and Mossbauer spectroscopies. With a total molecular mass ranging from 150 to 220 kDa, APS reductases have a subunit composition of the type 012)32 or 02)3. The subunit molecular mass is approximately 70 and 20 kDa for the a and )3 subunits, respectively. Amino-acid sequence data suggest that both iron-sulfur clusters are located in the (3 subunit... 

D. desulfuricans is able to grow on nitrate, inducing two enzymes that responsible for the steps of conversion of nitrate to nitrite (nitrate reductase-NAP), which is an iron-sulfur Mo-containing enzyme, and that for conversion of nitrite to ammonia (nitrite reduc-tase-NIR), which is a heme-containing enzyme. Nitrate reductase from D. desulfuricans is the only characterized enzyme isolated from a sulfate reducer that has this function. The enzyme is a monomer of 74 kDa and contains two MGD bound to a molybdenum and one [4Fe-4S] center (228, 229) in a single polypeptide chain of 753 amino acids. FXAFS data on the native nitrate reductase show that besides the two pterins coordinated to the molybdenum, there is a cysteine and a nonsulfur ligand, probably a Mo-OH (G. N. George, personal communication). 

FPR studies at low temperature detect the presence of one iron-sulfur center and molybdenum. At low temperature a sample of nitrate reductase reduced by dithionite shows a rhombic signal (gm,x = 2.04, gmed = 1.94, and gnm = 1.90). This signal accounts for 0.84 spins/... 

Fig. 6. Representative EPR spectra displayed by trinuclear and tetranucleEir iron-sulfur centers, (a) and (b) [3Fe-4S] + center in the NarH subunit of Escherichia coli nitrate reductase and the Ni-Fe hydrogenase fromD. gigas, respectively, (c) [4Fe-4S] + center in D. desulfuricans Norway ferredoxin I. (d) [4Fe-4S] center in Thiobacillus ferrooxidans ferredoxin. Experimental conditions temperature, 15 K microwave frequency, 9.330 GHz microwave power, (a) 100 mW, (b) 0.04 mW, (c) smd (d) 0.5 mW modulation amplitude (a), (c), (d) 0.5 mT, (b) 0.1 mT.

Similar difficulties have been encountered in the case of complex enzymes such as fumarate reductase and nitrate reductase from E. coli, in which substituting certain Cys ligands led to the loss of several if not all the iron-sulfur centers (171, 172). However, in the case of nitrate reductase, which possesses one [3Fe-4S] and three [4Fe-4S] centers, it was possible to remove selectively one [4Fe-4S]... 

The conversion of a [3Fe-4S] into a [4Fe-4S] center was achieved by restoring the second residue of the consensus motif in E. coli fu-marate reductase (181) and in D. africanus ferredoxin III (161). However, the coordination scheme of the iron-sulfur centers of A. vinelan-... 

H)2-D3 is a weak agonist and must be modified by hydroxylation at position Cj for full biologic activity. This is accomplished in mitochondria of the renal proximal convoluted tubule by a three-component monooxygenase reaction that requires NADPFl, Mg, molecular oxygen, and at least three enzymes (1) a flavoprotein, renal ferredoxin reductase (2) an iron sulfur protein, renal ferredoxin and (3) cytochrome P450. This system produces l,25(OH)2-D3, which is the most potent namrally occurring metabolite of vitamin D. 

The conditions under which these function and their regulation depend on the organism. For example, in Escherichia coli, oxygen represses the synthesis of the other reductases, and under anaerobic conditions the reductases for fumarate, DMSO, and TMAO are repressed by nitrate. This does not apply to Wolinella succinogenes in which sulfur represses the synthesis of the more positive electron acceptors nitrate and fumarate (Lorenzen et al. 1993). The DMSO reductase from Escherichia coli (Weiner et al. 1988) has a broad substrate versatility, and is able to reduce a range of sulfoxides and A-oxides. Anaerobic sulfate reduction is not discussed here in detail. 

Wan J, TK Tokunaga, E Brodie, Z Wang, Z Zheng, D Herman, TC Hazen, MK Firestone, SR Sutton (2005) Reoxidation of bioreduced uranium under reducing conditions. Environ Sci Technol 39 6162-6169. Weiner JH, DP Macisaac, RE Bishop, PT Bilous (1988) Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity J Bacterial 170 1505-1510. 

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