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. 2001 Apr 10;98(9):5013–5018. doi: 10.1073/pnas.081088398

Figure 5.

Figure 5

A schematic model explaining the experimental data in terms of structural events. In the wild-type enzyme, the protonated, charged (+) K(I-362) forms a hydrogen bond with a water molecule, which is hydrogen bonded to S(I-299). Formation of Pr involves the transfer of an additional electron to the binuclear center. To compensate for this negative charge, the K(I-362) side chain has to move toward the binuclear center.