Carbon monoxide-driven electron transport in Clostridium thermoautotrophicum membranes.
Membrane vesicles of Clostridium thermoautotrophicum prepared by osmotic lysis after lysozyme treatment contained carbon monoxide dehydrogenase and methylenetetrahydrofolate dehydrogenase with specific activities three- to fourfold higher than the specific activity of the cytoplasm. The membrane-associated carbon monoxide dehydrogenase mediated the reduction with CO or the oxidation with CO2 of b-type cytochromes and other electron carriers in the membrane.
Hugenholtz
J
J
Department of Biochemistry, University of Georgia, Athens 30602.
Ivey
D M
DM
Ljungdahl
L G
LG
D000445:Aldehyde Oxidoreductases / Q000378:metabolism*; D002248:Carbon Monoxide / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism; D003013:Clostridium / Q000201:enzymology / Q000378:metabolism* / Q000648:ultrastructure; D003580:Cytochromes / Q000378:metabolism; D004579:Electron Transport; D042965:Methylenetetrahydrofolate Reductase (NADPH2); D009097:Multienzyme Complexes; D010084:Oxidation-Reduction; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*
D003580:Cytochromes; D009097:Multienzyme Complexes; D002248:Carbon Monoxide; D000445:Aldehyde Oxidoreductases; C019823:carbon monoxide dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors; D042965:Methylenetetrahydrofolate Reductase (NADPH2)