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

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.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Agmon N,Doster W,Post F

doi

10.1016/S0006-3495(94)80953-1

subject

Has Abstract

pub_date

1994-05-01 00:00:00

pages

1612-22

issue

5

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(94)80953-1

journal_volume

66

pub_type

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