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

Author:

D'Mello R1,Hill S1,Poole R K1

Affiliation:

1. Division of Life Sciences, King's College London, United Kingdom.

Abstract

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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference32 articles.

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5. Properties of terminal oxidase systems of bacteroids from root nodules of soybean and cowpea and of N2-fixing bacteria grown in continuous culture;Bergersen F. J.;J. Gen. Microbiol.,1980

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