First evidence for existence of an uphill electron transfer through the bc(1) and NADH-Q oxidoreductase complexes of the acidophilic obligate chemolithotrophic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans.
The energy-dependent electron transfer pathway involved in the reduction of pyridine nucleotides which is required for CO(2) fixation to occur in the acidophilic chemolithotrophic organism Thiobacillus ferrooxidans was investigated using ferrocytochrome c as the electron donor. The experimental results show that this uphill pathway involves a bc(1) and an NADH-Q oxidoreductase complex functioning in reverse, using an electrochemical proton gradient generated by ATP hydrolysis. Based on these results, a model is presented to explain the balance of the reducing equivalent from ferrocytochrome c between the exergonic and endergonic electron transfer pathways.
Elbehti
A
A
Bioénergétique et Ingénierie des Proteines, CNRS, Institut de Biologie Structurale et Microbiologie, 13402 Marseille, cedex 20, France.
Brasseur
G
G
Lemesle-Meunier
D
D
D001693:Biological Transport, Active; D003574:Cytochrome c Group / Q000378:metabolism; D004579:Electron Transport; D042967:Electron Transport Complex I; D014450:Electron Transport Complex III / Q000378:metabolism*; D004734:Energy Metabolism; D005296:Ferrous Compounds / Q000378:metabolism; D009243:NAD / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D013855:Thiobacillus / Q000201:enzymology* / Q000378:metabolism
D003574:Cytochrome c Group; D005296:Ferrous Compounds; D009243:NAD; D009247:NADH, NADPH Oxidoreductases; D042967:Electron Transport Complex I; D014450:Electron Transport Complex III; D010100:Oxygen