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Circumstantial Evidence for Cytochromeb1Involvement in the Functioning of lac-Permease in RespiringEscherichia coli

Authors
Journal
Journal of Theoretical Biology
0022-5193
Publisher
Elsevier
Publication Date
Volume
182
Issue
4
Identifiers
DOI: 10.1006/jtbi.1996.0187
Disciplines
  • Biology

Abstract

Abstract The structure of the haem-binding site of cytochrome b 1and particularly the fact that the two protein ligands of the haem are methionines could explain a correlation found between loss of lac-permease activity and replacement of methionine by norleucine in the protein of aerobically respiring E. coli. If cytochrome b 1is essential for lac-permease mediated transport in whole bacteria as this correlation suggests, translocation of substrate by this permease must be coupled to electron transport. Such a dependence would invalidate the chemiosmotic interpretation of lactose transport in E. coliin its present form and would be in variance with the coupling-by-energy theories of lactose transport that exempted translocation from dependence on energy yielding processes.

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