THE OXYGEN-AFFINITY OF CYTOCHROME BO' IN ESCHERICHIA-COLI DETERMINED BY THE DEOXYGENATION OF OXYLEGHEMOGLOBIN AND OXYMYOGLOBIN - K-M VALUESFOR OXYGEN ARE IN THE SUBMICROMOLAR RANGE
R. Dmello et al., THE OXYGEN-AFFINITY OF CYTOCHROME BO' IN ESCHERICHIA-COLI DETERMINED BY THE DEOXYGENATION OF OXYLEGHEMOGLOBIN AND OXYMYOGLOBIN - K-M VALUESFOR OXYGEN ARE IN THE SUBMICROMOLAR RANGE, Journal of bacteriology, 177(3), 1995, pp. 867-870
Apparent oxygen affinities for Escherichia coli cells and membranes co
ntaining a terminal oxidase,vith only one type of ligand-binding heme,
cytochrome o', were measured with oxyleghemoglobin and oxymyoglobin a
s sensitive oxygen reporters. Two K-m values (0.15 to 0.35 mu M and 0.
016 to 0.085 mu M) were detected, well below values determined for the
purified oxidase by insensitive electrode methods.