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Overexpression, purification, and enthalpy of unfolding of ferricytochrome c552 from a psychrophilic microorganism.


ABSTRACT: The psychrophilic, hydrocarbonoclastic microorganism Colwellia psychrerythraea is important in global nutrient cycling and bioremediation. In order to investigate how this organism can live so efficiently at low temperatures (~4°C), thermal denaturation studies of a small electron transfer protein from Colwellia were performed. Colwellia cytochrome c552 was overexpressed in Escherichia coli, isolated, purified, and characterized by UV-visible absorption spectroscopy. The melting temperature (Tm) and the van't Hoff enthalpy (?HvH) were determined. These values suggest an unexpectedly high stability for this psychrophilic cytochrome.

SUBMITTER: Oswald VF 

PROVIDER: S-EPMC3885257 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature

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Overexpression, purification, and enthalpy of unfolding of ferricytochrome c552 from a psychrophilic microorganism.

Oswald Victoria F VF   Chen WeiTing W   Harvilla Paul B PB   Magyar John S JS  

Journal of inorganic biochemistry 20131112


The psychrophilic, hydrocarbonoclastic microorganism Colwellia psychrerythraea is important in global nutrient cycling and bioremediation. In order to investigate how this organism can live so efficiently at low temperatures (~4°C), thermal denaturation studies of a small electron transfer protein from Colwellia were performed. Colwellia cytochrome c552 was overexpressed in Escherichia coli, isolated, purified, and characterized by UV-visible absorption spectroscopy. The melting temperature (Tm)  ...[more]

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