PMID:9446680

Citation	Herter, SM, Kortlüke, CM and Drews, G (1998) Complex I of Rhodobacter capsulatus and its role in reverted electron transport. Arch. Microbiol. 169:98-105
Abstract	The activities of NAD+-photoreduction and NADH/decyl-ubiquinone reductase in membrane preparations of Rhodobacter capsulatus changed to the same extent under different conditions. These results indicated that NADH:ubiquinone oxidoreductase (complex I) catalyzes the electron transport in the downhill direction (respiratory chain) and in the uphill direction (reverted electron flow). This conclusion was confirmed by the characterization of a complex-I-deficient mutant of R. capsulatus. The mutant was not able to reduce NAD+ in the light. Since this mutant was not able to grow photoautotrophically, we concluded that complex I is the enzyme that catalyzes the reverted electron flow to NAD+ to provide reduction equivalents for CO2 fixation. Complex I is not essential for the reverted electron flow to nitrogenase since the mutant grew under nitrogen-fixing conditions. As shown by immunological means, NuoE, a subunit of complex I from R. capsulatus having an extended C-terminus, was modified depending on the nitrogen source present in the growth medium. When the organism used N2 instead of NH4+, a smaller NuoE polypeptide was synthesized. The complex-I-deficient mutant was not able to modify NuoE. The function of the modification is discussed.
Links	PubMed
Keywords	Electron Transport; Multigene Family; Mutation; NAD/metabolism; NAD(P)H Dehydrogenase (Quinone)/metabolism; Rhodobacter capsulatus/genetics; Rhodobacter capsulatus/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
RHOCB:D5ATH7		GO:0050136: NADH dehydrogenase (quinone) activity	ECO:0000314:		F		Figure 1	complete CACAO 8881

References

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