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. 1994 May;66(5):1612–1622. doi: 10.1016/S0006-3495(94)80953-1

The transition from inhomogeneous to homogeneous kinetics in CO binding to myoglobin.

N Agmon 1, W Doster 1, F Post 1
PMCID: PMC1275881  PMID: 8061210

Abstract

Heme proteins react inhomogeneously with ligands at cryogenic temperatures and homogeneously at room temperature. We have identified and characterized a transition from inhomogeneous to homogeneous behavior at intermediate temperatures in the time dependence of CO binding to horse myoglobin. The turnover is attributed to a functionally important tertiary protein relaxation process during which the barrier increases dynamically. This is verified by a combination of theory and multipulse measurements. A likely biological significance of this effect is in the autocatalysis of the ligand release process.

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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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