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J. Biol. Chem., Vol. 268, Issue 2, 815-822, Jan, 1993
DJ Westenberg, RP Gunsalus, BA Ackrell, H Sices and G Cecchini
Escherichia coli fumarate reductase (FRD) is a four-subunit enzyme that
catalyzes the terminal step in anaerobic respiration to fumarate. The
hydrophobic FrdC and FrdD subunits anchor the FrdA and FrdB catalytic
subunits to the inner surface of the cytoplasmic membrane and are required
for the enzyme to interact with quinones. Thirty-five single- site
mutations were constructed in the FrdC and FrdD polypeptides by
site-directed mutagenesis. Each mutant enzyme was characterized for its
ability to catalyze quinone oxidation and reduction and to support growth
of E. coli DW35 (delta frdABCD sdhC::kan) under selective conditions
requiring functional enzyme. Replacement of FrdCE29 with Asp, Leu, Lys, or
Phe had a deleterious effect both on quinol oxidase and quinone reductase
activities. Substitution of FrdCH82 with Arg, Leu, Tyr, or Glu also
decreased menaquinol oxidase activity, but had variable effects on the
reverse reaction, the reduction of ubiquinone. Data are presented to
support the hypothesis that the positive charge at FrdCH82 is required for
stabilization of the quinone radical intermediate and the negative charge
at FrdCE29 for deprotonation of menaquinol. Other critical amino acids
identified in FrdC included Ala- 32, Phe-38, Trp-86, Phe-87, and in FrdD
residues Phe-57, Gln-59, Ser- 60, and His-80. The established roles of such
residues in the QA and QB sites of the photosynthetic reaction center would
suggest a similar type of structure operative in the FRD complex. In such a
model, Glu- 29, Ala-32, His-82, Trp-86 of FrdC and His-80 of FrdD are
considered participants in a QB-type site, and FrdD Phe-57, Gln-59, and
Ser-60 components in an apolar QA-type site.
Escherichia coli fumarate reductase frdC and frdD mutants. Identification of amino acid residues involved in catalytic activity with quinones
Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90024.
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