Ferredoxin oxidoreductase

Mukund S, MWW Adams (1991) The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. J Biol Chem 266 14208-14216. 

Mukund S, MWW Adams (1995) Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. J Biol Chem 270 8389-8392. 

Roy R, S Mukund, GJ Schut, DM Dunn, R Weiss, MWW Adams (1999) Purification and molecular characterization of the tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus the third of a putative five-member tungstoenzyme family. J Bacteriol 181 1171-1180. 

Dorner E, M Boll (2002) Properties of 2-oxoglutarate ferredoxin oxidoreductase from Thauera aromatica and its role in enzymatic reduction of the aromatic ring. J Bacterial 184 3975-3983. 

Luo J, Fukuda E, Takase H et al (2009) Identification of the lysine residue responsible for coenzyme A binding in the heterodimeric 2-oxoacid ferredoxin oxidoreductase from Sulfo-lobus tokodaii, a thermoacidophilic archaeon, using 4-fluoro-7-nitrobenzofurazan as an affinity label. Biochim Biophys Acta 1794 335-340... 

Chan, M.K., S. Mukund, A. Kletzin, M.W. Adams, and D.C. Rees. 1995. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267 1463-1469. 

Ferredoxins are electron-transfer proteins that can mediate between pyruvate ferredoxin oxidoreductase and hydrogenase. It appears that during the course of the evolution, different types of ferredoxin were recruited for this purpose. In Clostridia, ferredoxins of the 2[4Fe-4S] type are used (Uyeda and Rabinowitz 1971). In T. vaginalis (Chapman et al. 1986) and T. foetus (Marczak et al. 1983), [2Fe-2S] ferredoxins are used. Their axial EPR spectra at g = 1.94,2.02 (Fig. 9.2) resemble those of the ferredoxins that are involved in P450 monooxygenase systems. Similar ferredoxins, with various functions, have been isolated from... 

Uyeda K, Rabinowitz JC. 1971. Pyruvate-ferredoxin oxidoreductase III. Purification and properties of the enzyme. J Biol Chem 246 311-19. 

Ferredoxins (Fds) are widespread in the three domains of life and an abundance of sequence data and structural information are available for Fds isolated from several sources. In particular, the bacterial type Fds are small electron-transfer proteins that posses cubane xFe-yS clusters attached to the protein matrix by Fe ligation of Cys via a conserved consensus ligating sequence. The archaeal type ferredoxins are water-soluble electron acceptors for the acyl-coenzyme A forming 2-oxoacid/ferredoxin oxidoreductase, a key enzyme involved in the central archaeal metabolic pathways. Fds have been distinguished according to the number of iron and inorganic sulphur atoms, 2Fe-2S, 4Fe-4S/3Fe-4S (Fig. Ib-d) and Zn-containing Fds. 

Pyrimidinethione complexes, osmium, 37 296 Pyriminethionate, as bridging ligands in platinum dimers, 40 202-205 Pyrochlores, 17 108 Pyrococcus furiosus, 38 344-383 aldehyde ferredoxin oxidoreductase, 38 374-381... 

Mechanism of Action An ant iparasiticthat interferes with the body s reaction to pyruvate ferredoxin oxidoreductase, an enzyme essential for anaerobic energy metabolism. Therapeutic Effect Produces antiprotozoal activity, reducing or terminating diarrheal episodes. 

Both hydrogenase and pyruvate-ferredoxin oxidoreductase activities were inhibited in nitrite-treated cells, and the inhibition was greater with addition of both nitrite and ascorbate (Payne et al., 1990a). However, they noted that enzyme inhibition was not complete. Meyer (1981) also reported incomplete in-... 

Based on the incomplete inhibition of iron-sulfur proteins by nitrite, and the observation that low-spin Fe—NO EPR signals were observed by C. sporogenes cultures that recovered from nitrite treatment, Payne et al. (1990a) concluded that the antimicrobial effect of nitrite or NO cannot be explained by direct inhibition of preformed pyruvate—ferredoxin oxidoreductase or hydrogenase. 

Carpenter, C. E., Reddy, D. S. A., and Cornforth, D. P. (1987). Inactivation of clostridial ferredoxin and pyruvate-ferredoxin oxidoreductase by sodium nitrite. Appl. Environ. Microbiol. 53, 549-552. 

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