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Figure 2.
Fig. 2. Redox-coupled conformational changes in Asp-51. (A)
Stereoscopic drawing of the hydrogen-bond network in the fully
oxidized and reduced (blue structure) states at 1.8- and
1.9-Å resolution, respectively, viewed from the
intermembrane side. The two histidines bound to Fe[a] (heme a
iron), are not shown. (B) The hydrogen-bonding structure of
Asp-51 in the oxidized (Left) and reduced (Right) states. The
smooth thick curve denotes the molecular surface to which the
water molecules in the intermembrane space are accessible. The
conformational changes induced by reduction of the enzyme are
shown by blue structures in Right. The blue (A) and black (B)
balls represent the fixed water molecules. The dotted lines
denote hydrogen bonds. The double-headed dotted arrows show a
possible movement of the water molecule from Arg-38 to Tyr-371.
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