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Transmembrane movement of heme.

W R Light¹, J S Olson

¹Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77251.

The Journal of Biological Chemistry

|September 15, 1990

Summary

This study demonstrates that carbon monoxide-heme (CO-heme) partitions into and across lipid bilayers. Kinetic and chromatographic methods reveal distinct phases for CO-heme binding and transmembrane movement within membranes.

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Area of Science:

Biochemistry
Membrane Biophysics
Physical Chemistry

Background:

Understanding how small molecules like heme interact with and traverse biological membranes is crucial for pharmacology and cell biology.
Carbon monoxide-heme (CO-heme) serves as a model for studying heme dynamics in lipid environments.

Purpose of the Study:

To investigate the kinetics and mechanisms of CO-heme partitioning into and across lipid bilayers.
To differentiate between initial binding to the membrane surface and transmembrane translocation of CO-heme.

Main Methods:

Stopped-flow spectroscopy to monitor rapid kinetic events.
Stopped-flow spectroscopy combined with rapid mixing techniques.
Column chromatography for isolating bound heme fractions.
Kinetic analysis of CO-heme binding and dissociation with lipid vesicles and apomyoglobin.

Main Results:

Biphasic kinetic time courses indicated distinct binding and translocation steps for CO-heme.
The initial rapid phase correlated with CO-heme partitioning to the outer lipid layer.
A slower phase, independent of heme and lipid concentration, represented transmembrane movement, accounting for up to 45% of the absorbance change.
Transmembrane movement rate was sensitive to acyl chain length, unlike initial binding.

Conclusions:

The study provides strong evidence for transmembrane movement of CO-heme across lipid bilayers.
Two kinetically distinct heme fractions, surface-bound and translocated, were identified and could be chromatographically separated.
The findings elucidate the complex dynamics of heme within lipid membrane environments.

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