ArticleJournal of inorganic biochemistry2014
Overexpression, purification, and enthalpy of unfolding of ferricytochrome c552 from a psychrophilic microorganism.
Article in Journal of inorganic biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 7 citations in OpenAlex.
- Helping proteins come in from the cold: 5 burning questions about cold-active enzymes.BBA advances · 2024Review
- Activity-stability relationships revisited in blue oxidases catalyzing electron transfer at extreme temperatures.Extremophiles : life under extreme conditions · 2016Article
- The structure of ferricytochrome c552 from the psychrophilic marine bacterium Colwellia psychrerythraea 34H.Metallomics : integrated biometal science · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
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.
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