Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/88971
Title: Isolation and characterization of a hybrid respiratory supercomplex consisting of Mycobacterium tuberculosis cytochrome bcc and Mycobacterium smegmatis cytochrome aa3
Authors: Berry, Edward A.
Huang, Li-Shar
Kim, Mi-Sun
Jang, Jichan
Pethe, Kevin
Nurlilah AB Rahman
Keywords: Enzyme Purification
Electron Transfer Complex
DRNTU::Science::Medicine
Issue Date: 2015
Source: Kim, M.-S., Jang, J., Nurlilah AB Rahman, Pethe, K., Berry, E. A., & Huang, L.-S. (2015). Isolation and characterization of a hybrid respiratory supercomplex consisting of Mycobacterium tuberculosis cytochrome bcc and Mycobacterium smegmatis cytochrome aa3. Journal of Biological Chemistry, 290(23), 14350-14360. doi:10.1074/jbc.M114.624312
Series/Report no.: Journal of Biological Chemistry
Abstract: Recently, energy production pathways have been shown to be viable antitubercular drug targets to combat multidrug-resistant tuberculosis and eliminate pathogen in the dormant state. One family of drugs currently under development, the imidazo[1,2-a]pyridine derivatives, is believed to target the pathogen's homolog of the mitochondrial bc1 complex. This complex, denoted cytochrome bcc, is highly divergent from mitochondrial Complex III both in subunit structure and inhibitor sensitivity, making it a good target for drug development. There is no soluble cytochrome c in mycobacteria to transport electrons from the bcc complex to cytochrome oxidase. Instead, the bcc complex exists in a “supercomplex” with a cytochrome aa3-type cytochrome oxidase, presumably allowing direct electron transfer. We describe here purification and initial characterization of the mycobacterial cytochrome bcc-aa3 supercomplex using a strain of M. smegmatis that has been engineered to express the M. tuberculosis cytochrome bcc. The resulting hybrid supercomplex is stable during extraction and purification in the presence of dodecyl maltoside detergent. It is hoped that this purification procedure will potentiate functional studies of the complex as well as crystallographic studies of drug binding and provide structural insight into a third class of the bc complex superfamily.
URI: https://hdl.handle.net/10356/88971
http://hdl.handle.net/10220/46060
ISSN: 0021-9258
DOI: 10.1074/jbc.M114.624312
Rights: © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.. Author's Choice—Final version free via Creative Commons CC-BY license.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:LKCMedicine Journal Articles

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