An Investigation into Membrane Bound Redox Carriers Involved in Energy Transduction Mechanism in Brevibacterium linens DSM 20158 with Unsequenced Genome
Brevibacterium linens (B. linens) DSM 20158 with an unsequenced genome can be used as a non-pathogenic model to study features it has in common with other unsequenced pathogens of the same genus on the basis of comparative proteome analysis. The most efficient way to kill a pathogen is to target its energy transduction mechanism. In the present study, we have identified the redox protein complexes involved in the electron transport chain of B. linens DSM 20158 from their clear homology with the shot-gun genome sequenced strain BL2 of B. linens by using the SDS–Polyacrylamide gel electrophoresis coupled with nano LC–MS/MS mass spectrometry. B. linens is found to have a branched electron transport chain (Respiratory chain), in which electrons can enter the respiratory chain either at NADH (Complex I) or at Complex II level or at the cytochrome level. Moreover, we are able to isolate, purify, and characterize the membrane bound Complex II (succinate dehydrogenase), Complex III (menaquinone cytochrome c reductase cytochrome c subunit, Complex IV (cytochrome c oxidase), and Complex V (ATP synthase) of B. linens strain DSM 20158.
KeywordsRedox proteins Cytochromes Isolation Purification Characterization Proteomics
We would like to thank the Wellcome Trust for funding the purchase of the ABSciex QStar XL mass spectrometer and The Higher Education Commission (HEC), Pakistan is thanked for scholarship (IRSIP) funding to KS.
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