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. 1974 Feb;71(2):558–562. doi: 10.1073/pnas.71.2.558

The Kinetics of Conformational Changes in Hemoglobin, Studied by Laser Photolysis

B Alpert *, R Banerjee *, L Lindqvist †
PMCID: PMC388047  PMID: 4521822

Abstract

Photolysis of carbon monoxide and oxygen derivatives of hemoglobin by a short laser pulse produces a transient species that rapidly decays to normal deoxyhemoglobin. The effect, which is also observed on single chain proteins and on noncooperative aggregated forms, has been interpreted as corresponding to structural changes in the heme pocket on ligand dissociation. The decay of the transient species follows first-order kinetics with constants ranging from 0.8 to 1.8 × 107 sec-1. In cooperative hemoglobins, the kinetic constants are pH-dependent, though remaining first- or pseudo first-order at all wavelengths. This shows the close linkage of tertiary and quaternary structure changes in normal hemoglobin.

Keywords: myoglobin, cooperative interactions, ligand binding

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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