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Main Title: Domain motions and electron transfer dynamics in 2Fe-superoxide reductase
Author(s): Horch, Marius
Utesch, Tillmann
Hildebrandt, Peter
Mroginski, Maria Andrea
Zebger, Ingo
Type: Article
Language Code: en
Abstract: Superoxide reductases are non-heme iron enzymes that represent valuable model systems for the reductive detoxification of reactive oxygen species. In the present study, we applied different theoretical methods to study the structural dynamics of a prototypical 2Fe-superoxide reductase and its influence on electron transfer towards the active site. Using normal mode and essential dynamics analyses, we could show that enzymes of this type are capable of well-defined, electrostatically triggered domain movements, which may allow conformational proofreading for cellular redox partners involved in intermolecular electron transfer. Moreover, these global modes of motion were found to enable access to molecular configurations with decreased tunnelling distances between the active site and the enzyme's second iron centre. Using all-atom classical molecular dynamics simulations and the tunnelling pathway model, however, we found that electron transfer between the two metal sites is not accelerated under these conditions. This unexpected finding suggests that the unperturbed enzymatic structure is optimized for intramolecular electron transfer, which provides an indirect indication of the biological relevance of such a mechanism. Consistently, efficient electron transfer was found to depend on a distinct route, which is accessible via the equilibrium geometry and characterized by a quasi conserved tyrosine that could enable multistep-tunnelling (hopping). Besides these explicit findings, the present study demonstrates the importance of considering both global and local protein dynamics, and a generalized approach for the functional analysis of these aspects is provided.
Issue Date: 2016
Date Available: 24-Oct-2017
DDC Class: 540 Chemie und zugeordnete Wissenschaften
Sponsor/Funder: DFG, EXC 314, Unifying Concepts in Catalysis
Journal Title: Physical chemistry, chemical physics
Publisher: Royal Society of Chemistry
Publisher Place: Cambridge
Volume: 18
Issue: 33
Publisher DOI: 10.1039/c6cp03666j
Page Start: 23053
Page End: 23066
EISSN: 1463-9084
ISSN: 1463-9076
Appears in Collections:FG Physikalische Chemie / Biophysikalische Chemie » Publications

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