ArticleScientific reports2024
Temperature-dependent iron motion in extremophile rubredoxins - no need for 'corresponding states'.
Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Crystallography of Extremophile Proteins-Structural Comparisons of Psychrophilic and Hyperthermophilic Rubredoxins.Biomolecules · 2026Article
- Practical issues in nuclear resonant vibrational spectroscopy for measuring biological samples: special problems, solutions and some perspectives.Applied spectroscopy reviews · 2025Article
- Changes in flexibility but not in compactness underlie the thermal adaptation of prokaryotic adenylate kinases.Evolution letters · 2025Article
- NRVS of FeS cluster proteins & models - A bestiary of nifty normal modes.Journal of inorganic biochemistry · 2025Review
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Authors and funding
17 authors.
Funding
Abstract
Extremophile organisms are known that can metabolize at temperatures down to - 25 °C (psychrophiles) and up to 122 °C (hyperthermophiles). Understanding viability under extreme conditions is relevant for human health, biotechnological applications, and our search for life elsewhere in the universe. Information about the stability and dynamics of proteins under environmental extremes is an important factor in this regard. Here we compare the dynamics of small Fe-S proteins - rubredoxins - from psychrophilic and hyperthermophilic microorganisms, using three different nuclear techniques as well as molecular dynamics calculations to quantify motion at the Fe site. The theory of 'corresponding states' posits that homologous proteins from different extremophiles have comparable flexibilities at the optimum growth temperatures of their respective organisms. Although 'corresponding states' would predict greater flexibility for rubredoxins that operate at low temperatures, we find that from 4 to 300 K, the dynamics of the Fe sites in these homologous proteins are essentially equivalent.
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