Temperature-Dependent Iron Motion in Extremophile Rubredoxins – No Need for ‘Corresponding States’
Author:
Cramer Stephen1, Jenney Francis2, Wang Hongxin1, George Simon1, Xiong Jin3, Guo Yisong3, Gee Leland4, Marizcurrena Juan5, Castro-Sowinski Susana5, Staskiewicz Anna2, Yoda Yoshitaka6, Hu Michael7, Tamasaku Kenji8, Nagasawa Nobumoto9, Li Lei10, Doukov Tzanko4, Matsuura Hiroaki8
Affiliation:
1. SETI Institute 2. PCOM Georgia 3. Carnegie Mellon University 4. SLAC 5. University of the Republic 6. Japan Synchrotron Radiation Research Institute 7. Argonne National Laboratory 8. RIKEN SPring-8 Center 9. SPring-8 10. Synchrotron Radiation Research Center,Hyogo Science and Technology Association
Abstract
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 4K to 300K, the dynamics of the Fe sites in these homologous proteins are essentially equivalent.
Publisher
Research Square Platform LLC
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