# Response to nitrosative stress of Escherichia coli

Wang, Jing (2015). Response to nitrosative stress of Escherichia coli. University of Birmingham. Ph.D.

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## Abstract

$$Escherichia$$ $$coli$$ encounters nitrosative stress from various sources. It was shown in a previous study that a possible role for Hcp in the nitrosative stress response. The focus of this study was to determine the function of Hcp. The growth of the $$hcp$$ mutant lacking all known NO reductases was inhibited by various sources of nitrosative stres. The growth defect was complemented by native Hcp protein, but not by mutated Hcp protein with a disrupted hybrid cluster. The role of Hcp was shown to protect $$E$$. $$coli$$ from nitrosative stress, and the hybrid cluster is critical for its function. Direct interaction between Hcp and its oxidoreductase Hcr was demonstrated. The $$hcp$$$$^+$$$$hcr$$ strain showed that it was still resistant to nitrosative stress. Possibly alternative oxidoreductase of Hcp exists in $$E$$. $$coli$$. Gas analysis of the headspace of the anaerobic cultures showed that when treated with NO, the Hcp$$^+$$ strain lacking all known NO reductases was still capable of reducing sub-micro molar NO into N$$_2$$O, while the further deletion of Hcp completely abolished NO reduction. This provides the first $$in$$ $$vivo$$ evidence that Hcp is a high affinity, low capacity NO reductase in $$E$$. $$coli$$.

Type of Work: Thesis (Doctorates > Ph.D.)
Award Type: Doctorates > Ph.D.
Supervisor(s):
Supervisor(s)EmailORCID
Cole, Jeffrey AlanUNSPECIFIEDUNSPECIFIED
Busby, SteveUNSPECIFIEDUNSPECIFIED
Licence:
College/Faculty: Colleges (2008 onwards) > College of Life & Environmental Sciences
School or Department: School of Biosciences
Funders: Other
Other Funders: China Scholarship Council
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QR Microbiology
URI: http://etheses.bham.ac.uk/id/eprint/6277

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