Literature DB >> 24275750

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

Victoria F Oswald1, WeiTing Chen1, Paul B Harvilla2, John S Magyar3.   

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 (ΔHvH) were determined. These values suggest an unexpectedly high stability for this psychrophilic cytochrome.
Copyright © 2013 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  Cytochrome c(552); Psychrophile; Thermal denaturation; Van't Hoff enthalpy

Mesh：

Substances：

Year:  2013        PMID： 24275750      PMCID： PMC3885257          DOI： 10.1016/j.jinorgbio.2013.11.002

Source DB:  PubMed          Journal:  J Inorg Biochem        ISSN： 0162-0134            Impact factor:   4.155


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1.  The structure of ferricytochrome c552 from the psychrophilic marine bacterium Colwellia psychrerythraea 34H.

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