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PMID:8944892
| Citation |
Yariv, J (1996) Circumstantial evidence for cytochrome b1 involvement in the functioning of lac-permease in respiring Escherichia coli. J. Theor. Biol. 182:459-62 |
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| Abstract |
The structure of the haem-binding site of cytochrome b1 and 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 b1 is 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. coli in 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. |
| Links |
PubMed Online version:10.1006/jtbi.1996.0187 |
| Keywords |
Bacterial Proteins; Biological Transport, Active; Cytochrome b Group/metabolism; Enzyme Activation; Escherichia coli/metabolism; Escherichia coli Proteins; Ferritins/metabolism; Lactose/metabolism; Membrane Transport Proteins/metabolism; Methionine/metabolism; Monosaccharide Transport Proteins; Oxygen Consumption; Symporters |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
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See also
References
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