Selenate reductase

Schroder I, S Rech, T Krafft, JM Macey (1997) Purification and characterization of the selenate reductase from Thauera selenatis. J Biol Chem 272 23765-23768. 

The selenate reductase from Enterobacter cloacae SLDla-1 functions only under aerobic conditions, and is not able to serve as an electron acceptor for anaerobic growth, in contrast to the periplasmic enzyme from Thauera selenatis (Schroder et al. 1997). In E. cloacae there are separate nitrate and selenate reductases, both of which are membrane-bound. The selenate reductase is able to reduce chlorate and bromate though not nitrate, contains Mo, heme and nonheme iron, and consists of three subunits in an a3p3y3 configuration. 

The chlorate reductase has been characterized in strain GR-1 where it was found in the periplasm, is oxygen-sensitive, and contains molybdenum, and both [3Fe-4S] and [4Fe-4S] clusters (Kengen et al. 1999). The arsenate reductase from Chrysiogenes arsenatis contains Mo, Fe, and acid-labile S (Krafft and Macy 1998), and the reductase from Thauera selenatis that is specific for selenate, is located in the periplasmic space, and contains Mo, Fe, acid-labile S, and cytochrome b (Schroeder et al. 1997). In contrast, the membrane-bound selenate reductase from Enterobacter cloacae SLDla-1 that cannot function as an electron acceptor under anaerobic conditions contains Mo and Fe and is distinct from nitrate reductase (Ridley et al. 2006). 

Included in Table I are molybdenum enzymes that are as yet unclassified due to their partial characterization (46—49, 58). These enzymes includes polysulfide reductase that accomplish sulfur reduction to sulfide (46), underlining its role in the global sulfur cycling. Chlorate and selenate reductase are examples of relatively rare enzymes using simple oxyanions of third-row elements as substrates (47 19, 58). 

The above schemes work reasonably well for certain enzyme reactions, especially for substrates where oxygen addition/loss occurs at a main group element (e.g., N, S, Se, Cl, see Table I). In addition to SO and nitrate reductase, key examples are DMSOR, trimethylamine oxide reductase, chlorate reductase, and selenate reductase. In the case of enzymes catalyzing C-based redox reactions of organic molecules, notably XDH and aldehyde oxidase, a direct OAT step is unlikely and is replaced by mechanistic steps typical of hydro-xylation (2). The essential features of the mechanism are shown in Fig. 10 for xanthine dehydrogenase/oxidase. 

Selenate reductase Enterobacter cloacae B-V Se04 " Psat = 0.2( 6.25 X 10 59... 

Another member of this family that has been studied by XAS is the selenate reductase from Thauera selenatisJ Like DMSO reduetase itself, this en me possesses a mono-oxo Mo(vi) site and a des-oxo Mo(iv) site with elose to four Mo-S ligands in both, eonsistentwith the coordination by two molybdopter-ins that is a signature of this family XAS also deteeted a low-valent selenium coordinated to an unknown metal ion (possibly iron) in the enzyme, although at the time of writing the role of this selenium remains unknown. 

The Butt group has reported direct electrochemistry of NapAB from Paracoccus pantotrophusf The same potential dependent catalytic currents seen for R. sphaeroid.es NapAB are also found for this system (Figure 5.27). In addition, significant selenate reductase activity was demonstrated for this enzyme. 

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