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 Previous Article

J. Bacteriol., 02 1995, 867-870, Vol 177, No. 3
Copyright © 1995, American Society for Microbiology

The oxygen affinity of cytochrome bo' in Escherichia coli determined by the deoxygenation of oxyleghemoglobin and oxymyoglobin: Km values for oxygen are in the submicromolar range

R D'Mello, S Hill and RK Poole
Division of Life Sciences, King's College London, United Kingdom.

Apparent oxygen affinities for Escherichia coli cells and membranes containing a terminal oxidase with only one type of ligand-binding heme, cytochrome o', were measured with oxyleghemoglobin and oxymyoglobin as sensitive oxygen reporters. Two Km values (0.15 to 0.35 microM and 0.016 to 0.085 microM) were detected, well below values determined for the purified oxidase by insensitive electrode methods.


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