Temperature-dependent iron motion in extremophile rubredoxins - no need for 'corresponding states'.

Autor: Jenney FE Jr; Georgia Campus, Philadelphia College of Osteopathic Medicine, Suwanee, GA, 30024, USA., Wang H; SETI Institute, Mountain View, CA, 94043, USA., George SJ; SETI Institute, Mountain View, CA, 94043, USA., Xiong J; Department of Chemistry, Carnegie Mellon University, Pittsburgh, PA, 15213, USA., Guo Y; Department of Chemistry, Carnegie Mellon University, Pittsburgh, PA, 15213, USA., Gee LB; LCLS, SLAC National Laboratory, Stanford, CA, 94025, USA., Marizcurrena JJ; Universidad de La República, Montevideo, Uruguay., Castro-Sowinski S; Universidad de La República, Montevideo, Uruguay., Staskiewicz A; Georgia Campus, Philadelphia College of Osteopathic Medicine, Suwanee, GA, 30024, USA., Yoda Y; Precision Spectroscopy Division, SPring-8/JASRI, Sayo, Hyogo, 679-5198, Japan., Hu MY; Advanced Photon Source, Argonne National Laboratory, Lemont, IL, 60439, USA., Tamasaku K; RIKEN/SPring-8 Center, Hyogo, 679-5148, Japan., Nagasawa N; Precision Spectroscopy Division, SPring-8/JASRI, Sayo, Hyogo, 679-5198, Japan., Li L; Synchrotron Radiation Research Center, Hyogo, 679-5165, Japan., Matsuura H; RIKEN/SPring-8 Center, Hyogo, 679-5148, Japan., Doukov T; SSRL, SLAC National Laboratory, Stanford, CA, 94025, USA., Cramer SP; SETI Institute, Mountain View, CA, 94043, USA. spjcramer@mac.com.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2024 May 28; Vol. 14 (1), pp. 12197. Date of Electronic Publication: 2024 May 28.
DOI: 10.1038/s41598-024-62261-2
Abstrakt: 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.
(© 2024. The Author(s).)
Databáze: MEDLINE
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