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The Local Environment of Iron Determines the Rupture Force of Rubredoxin and Not Hydrogen Bond Networks

submitted on 16.04.2020 and posted on 20.04.2020 by Maximilian Scheurer, Andreas Dreuw, Martin Head-Gordon, Tim Stauch

The surprisingly low rupture force and remarkable mechanical anisotropy of rubredoxin have been known for several years. Exploiting the first combination of steered molecular dynamics and the quantum chemical Judgement of Energy DIstribution (JEDI) analysis, the distribution of strain energy in the central part of rubredoxin is elucidated in real-time with unprecedented detail. In contrast to common belief that hydrogen bonds between neighboring amino acid backbones and the sulfur atoms of the central FeS4 unit in rubredoxin determine the low mechanical resistance of the protein, we demonstrate that structural anisotropy as well as the contribution of angle bendings in the FeS4 unit are instead the key factors responsible for the low rupture force in rubredoxin. In addition to clarifying the structural basis for the mechanical unfolding of an important metalloprotein, this study paves the way for in-depth investigations of an intriguing new class of mechanophores involving metal ions.


Deutsche Forschungsgemeinschaft GRK 1986, Complex Light Control

Heidelberg Graduate School of Mathematical and Computational Methods for the Sciences (GSC220)

National Institutes of Health, Grant No. 5U01GM121667

Deutsche Forschungsgemeinschaft STA 1526/1-1

Deutsche Forschungsgemeinschaft STA 1526/2-1


Email Address of Submitting Author


University of Bremen



ORCID For Submitting Author


Declaration of Conflict of Interest

The authors declare no conflict of interest.