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J Biol Chem, Vol. 273, Issue 48, 31916-31923, November 27, 1998
From the Department of Biochemistry and Molecular Biology, Oklahoma
State University, Stillwater, Oklahoma 74078
When purified ubiquinone (Q)-depleted
succinate-ubiquinone reductase from Escherichia coli is
photoaffinity-labeled with
3-azido-2-methyl-5-methoxy-[3H]6-geranyl-1,4-benzoquinone
([3H]azido-Q) followed by SDS-polyacrylamide gel
electrophoresis, radioactivity is found in the SdhC subunit, indicating
that this subunit is responsible for ubiquinone binding. An
[3H]azido-Q-linked peptide, with a retention time of 61.7 min, is obtained by high performance liquid chromatography of the
protease K digest of [3H]azido-Q-labeled SdhC obtained
from preparative SDS-polyacrylamide gel electrophoresis on labeled
reductase. The partial N-terminal amino acid sequence of this peptide
is NH2-TIRFPITAIASILHRVS-, corresponding to residues
17-33. The ubiquinone-binding domain in the proposed structural model
of SdhC, constructed based on the hydropathy plot of the deduced amino
acid sequence of this protein, is located at the N-terminal end toward
the transmembrane helix I. To identify amino acid residues responsible
for ubiquinone binding, substitution mutations at the putative
ubiquinone-binding region of SdhC were generated and characterized.
E. coli NM256 lacking genomic succinate-Q reductase genes
was constructed and used to harbor the mutated succinate-Q reductase
genes in a low copy number pRKD418 plasmid. Substitution of serine 27 of SdhC with alanine, cysteine, or threonine or substitution of
arginine 31 with alanine, lysine, or histidine yields cells unable to
grow aerobically in minimum medium with succinate as carbon source. Furthermore, little succinate-ubiquinone reductase activity and [3H]azido-Q uptake are detected in succinate-ubiquinone
reductases prepared from these mutant cells grown aerobically in LB
medium. These results indicate that the hydroxyl group, the size of the amino acid side chain at position 27, and the guanidino group at
position 31 of SdhC are critical for succinate-ubiquinone reductase activity, perhaps by formation of hydrogen bonds with carbonyl groups
of the 1,4-benzoquinone ring of the quinone molecule. The hydroxyl
group, but not the size of the amino acid side chain, at position 33 of
SdhC is also important, because Ser-33 can be substituted with
threonine but not with alanine.
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