An investigation into membrane bound redox carriers involved in energy transduction mechanism in Brevibacterium linens DSM 20158 with unsequenced genome

Shabbiri, Khadija, Botting, Catherine H., Adnan, Ahmad, Fuszard, Matthew, Naseem, Shahid, Ahmed, Safeer, Shujaat, Shahida, Syed, Quratulain and Ahmad, Waqar (2014) An investigation into membrane bound redox carriers involved in energy transduction mechanism in Brevibacterium linens DSM 20158 with unsequenced genome. Journal of Membrane Biology, 247 4: 345-355. doi:10.1007/s00232-014-9641-4


Author Shabbiri, Khadija
Botting, Catherine H.
Adnan, Ahmad
Fuszard, Matthew
Naseem, Shahid
Ahmed, Safeer
Shujaat, Shahida
Syed, Quratulain
Ahmad, Waqar
Title An investigation into membrane bound redox carriers involved in energy transduction mechanism in Brevibacterium linens DSM 20158 with unsequenced genome
Formatted title
An investigation into membrane bound redox carriers involved in energy transduction mechanism in Brevibacterium linens DSM 20158 with unsequenced genome
Journal name Journal of Membrane Biology   Check publisher's open access policy
ISSN 0022-2631
1432-1424
Publication date 2014-04
Sub-type Article (original research)
DOI 10.1007/s00232-014-9641-4
Open Access Status
Volume 247
Issue 4
Start page 345
End page 355
Total pages 11
Place of publication New York, NY, United States
Publisher Springer
Collection year 2015
Language eng
Formatted abstract
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.
Keyword Characterization
Cytochromes
Isolation
Proteomics
Purification
Redox proteins
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
School of Biological Sciences Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 0 times in Thomson Reuters Web of Science Article
Scopus Citation Count Cited 0 times in Scopus Article
Google Scholar Search Google Scholar
Created: Sun, 20 Apr 2014, 00:08:55 EST by System User on behalf of School of Biological Sciences