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Figure 2.
Fig. 2. The interactions of azide with catalytic side
chains in bovine F[1]-ATPase. The two negatively charged outer
nitrogen atoms of azide are hydrogen-bonded to  -Lys-162
and  -Arg-373, and the inner
positively charged nitrogen atom forms an ionic interaction with
the oxygen atom of the -phosphate of ADP. The
tight interaction between azide and the side chains prevents the
conversion of the subunit to the open conformation and the
release of ADP.
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