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The essential features of the “Perutz mechanism” of the T-R transition in hemoglobin

The essential features of the “Perutz mechanism” of the T-R transition in hemoglobin
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Description: The binding of oxygen to deoxyhemoglobin causes conformational changes in the heme.

In the deoxy state, heme has a dome shape.

Binding of the O2 ligand pulls the iron into the heme plane, flattening the heme and causing strain.

A shift in the orientation of His F8 relieves the strain, partly because Val FG5 is pushed to the right. In this way, the tertiary change in heme is communicated to the FG corner.

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