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

N. Agmon*, W. Doster, F. Post

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

40 Scopus citations

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.

Original languageEnglish
Pages (from-to)1612-1622
Number of pages11
JournalBiophysical Journal
Volume66
Issue number5
DOIs
StatePublished - 1994

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