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De novo design of symmetric ferredoxins that shuttle electrons in vivo. | LitMetric

De novo design of symmetric ferredoxins that shuttle electrons in vivo.

Proc Natl Acad Sci U S A

Environmental Biophysics and Molecular Ecology Program, Department of Marine and Coastal Sciences, Rutgers, The State University of New Jersey, New Brunswick, NJ 08901;

Published: July 2019

AI Article Synopsis

  • Researchers propose that the original symmetric structure of bacterial ferredoxins has changed over time due to gene duplication and mutations.
  • Phylogenetic studies suggest that the N- and C-terminal sequences of modern ferredoxins have evolved independently, allowing for the design of symmetric 4Fe-4S molecules that can bind [4Fe-4S] clusters.
  • The new symmetric ferredoxin designs show excellent electron transfer capabilities, demonstrating potential for use in metabolic pathways and applications in living organisms.

Article Abstract

A symmetric origin for bacterial ferredoxins was first proposed over 50 y ago, yet, to date, no functional symmetric molecule has been constructed. It is hypothesized that extant proteins have drifted from their symmetric roots via gene duplication followed by mutations. Phylogenetic analyses of extant ferredoxins support the independent evolution of N- and C-terminal sequences, thereby allowing consensus-based design of symmetric 4Fe-4S molecules. All designs bind two [4Fe-4S] clusters and exhibit strongly reducing midpoint potentials ranging from -405 to -515 mV. One of these constructs efficiently shuttles electrons through a designed metabolic pathway in These finding establish that ferredoxins consisting of a symmetric core can be used as a platform to design novel electron transfer carriers for in vivo applications. Outer-shell asymmetry increases sequence space without compromising electron transfer functionality.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6642340PMC
http://dx.doi.org/10.1073/pnas.1905643116DOI Listing

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