Perutz mechanism

Fig. 12. Schematic views of bis-histidyl ferri-, ferro-, and CO-ferro-heme-hemopexin. Unlike myoglobin with one open distal site, heme bound to hemopexin is coordinated to two strong field ligands, either of which a priori may be displaced by CO. This may well produce coupled changes in protein conformation like the Perutz mechanism for 02-binding by hemoglobin (143). The environment of heme bound to hemopexin and to the N-domain may be influenced by changes in the interactions of porphyrin-ring orbitals with those of aromatic residues in the heme binding site upon reduction and subsequent CO binding.

Perovskite, 253, 285 Perutz mechanism, 903 pH, and solvents, 322 Phorphorus pentafluoride, 205 Phosgene, 205... 

M. Perutz, Mechanisms of Cooperativity and Allosteric Regulation in Proteins," Cambridge University Press, Cambridge, 1990. 

Fig. 19.10 A schematic diagram i>l the Perutz mechanism ill hemoglobin. The three must important factors are highlighted 11) the environment of the heme (2) the movement pension) of the proiein chains, and (3) ihc breaking of hydrogen bonds ("salt bridges"). ICourtcsy of Professor M. Perutz. Reproduced with permission. ...

M.F. Perutz, Mechanisms of Cooperativity and Allosteric Regulation in Proteins. Q. Rev. Biophys., 22,139-236,1989. Reprinted in book form as referenced below (in ref. 16). 

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