Escherichia coli fumarate reductase

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. 

Cammack R, Patil DS, Weiner JH. 1986. Evidence that centre 2 in Escherichia coli fumarate reductase is a [4Fe-4S] cluster. Biochim Biophys Acta 870 545-51. 

Johnson MK, Morningstar JE, Cecchini G, Ackrell BAC. 1985. Detection of a tetranuclear iron sulphur centre in fumarate reductase from Escherichia coli by EPR. Arch Microbiol 131 756-62. 

Cole, S. T., 1982, Nucleotide sequence coding for the flavoprotein subunit of the fumarate reductase of Escherichia coli. Eur. J. Biochem. 122 479n484. 

Cole, S. T., Grundstrom, T., Jaurin, B., Robinson, J. J., and Weiner, J. H., 1982, Location and nucleotide sequence of frdB, the gene coding for the iron-sulphur protein subunit of the fumarate reductase of Escherichia coli. Eur. J. Biochem. 126 211n216. 

Iverson, T. M., Luna-Chavez, C., Cecchini, G., and Rees, D. C., 1999, Structure of the Escherichia coli fumarate reductase respiratory complex. Science 284 1961nl966. 

Westenberg, D. J., Gunsalus, R. P., Ackrell, B. A., Sices, H., and Cecchini, G., 1993, Escherichia coli fumarate reductase frdC and frdD mutants. Identification of amino acid residues involved in catalytic activity with quinones. J. Biol. Chem. 268 815n822. 

Guest, J. R., 1981, Partial replacement of succinate dehydrogenase function hy phage- and plasmid-specified fumarate reductase in Escherichia coli, J. Gen. Microbiol. 122 1719179. 

Maklashina, E., Berthold, D. A., and Cecchini, G., 1998, Anaerobic expression of Escherichia coli succinate dehydrogenase functional replacement of fumarate reductase in the respiratory chain during anaerobic growth, J. Bacteriol. 180(22) 5989n5996. 

Trinuclear clusters have been detected in over 20 proteins as well as a number of enzymes, among them aconitase, beef heart succinate-ubiquinone oxidoreductase (120), Escherichia coli nitrate reductase (121), E. coli fumarate reductase (122), and succinate dehydrogenase (123). Selected instances of the occurrence of [3Fe-4S] clusters are listed in Table II. Because of the paramagnetic ground states of both oxidation levels, these clusters can be uniquely identified by a number of spectroscopic techniques. Among these, Mossbauer spectroscopy in applied magnetic fields (124, 128, 132, 141-143) and low temperature MCD spectroscopy (127, 138, 144-146) are decisive. While there are small spectroscopic differences among certain [3Fe-4S] centers, the similarities dominate and support the essential structure 3 for all. In a number of the earlier papers on protein... 

Luna-Chavez, C., Iverson, T.M., Rees, D.C., and Cecchini, G., Overexpression, purification, and crystaUization of the membrane-bound fumarate reductase from Escherichia coli. Protein Exp. Purif., 19, 188, 2000. 

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