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J Biol Chem, Vol. 273, Issue 15, 9085-9093, April 10, 1998
From the Department of Biochemistry, Dartmouth Medical School,
Hanover, New Hampshire 03755 and the Universitätsklinikum
Frankfurt, ZBC, Institut für Biochemie I,
D-60590 Frankfurt, Germany
The crystal structure of the bovine Rieske
iron-sulfur protein indicates a sulfur atom (S-1) of the iron-sulfur
cluster and the sulfur atom (S Eliminating the hydrogen bond from the hydroxyl group of Ser-183 to S-1
of the cluster lowers the midpoint potential of the cluster by 130 mV,
and eliminating the hydrogen bond from the hydroxyl group of Tyr-185 to
S
Alteration of the Midpoint Potential and Catalytic Activity of
the Rieske Iron-Sulfur Protein by Changes of Amino Acids Forming
Hydrogen Bonds to the Iron-Sulfur Cluster
) of a cysteine
residue that coordinates one of the iron atoms form hydrogen bonds with
the hydroxyl groups of Ser-163 and Tyr-165, respectively. We have
altered the equivalent Ser-183 and Tyr-185 in the Saccharomyces
cerevisiae Rieske iron-sulfur protein by site-directed
mutagenesis of the iron-sulfur protein gene to examine how these
hydrogen bonds affect the midpoint potential of the iron-sulfur cluster
and how changes in the midpoint potential affect the activity of the
enzyme.
of Cys-159 lowers the midpoint potential by 65 mV.
Eliminating both hydrogen bonds has an approximately additive effect,
lowering the midpoint potential by 180 mV. Thus, these hydrogen bonds
contribute significantly to the positive midpoint potential of the
cluster but are not essential for its assembly. The activity of the
bc1 complex decreases with the decrease in
midpoint potential, confirming that oxidation of ubiquinol by the
iron-sulfur protein is the rate-limiting partial reaction in the
bc1 complex, and that the rate of this reaction
is extensively influenced by the midpoint potential of the iron-sulfur
cluster.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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