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Electrochemical Detection of Deuterium Kinetic Isotope Effect on Extracellular Electron Transport in Shewanella oneidensis MR-1

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Published on: April 16, 2018

Sco proteins are involved in electron transfer processes.

Lucia Banci¹, Ivano Bertini, Simone Ciofi-Baffoni

¹Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry

|December 25, 2010

Summary

Sco proteins, crucial for copper metabolism, exhibit diverse copper-binding affinities. This study reveals that the histidine ligand is key in determining whether a Sco protein acts as a metallochaperone or a redox enzyme.

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Area of Science:

Biochemistry
Structural Biology
Microbiology

Background:

Sco proteins possess a thioredoxin-like fold and are involved in copper homeostasis.
They bind copper ions with varying affinities, playing roles in copper chaperone and thioredoxin functions.
Their involvement in cytochrome c oxidase assembly is well-documented.

Purpose of the Study:

To structurally characterize a Sco domain fused with cytochrome c from Pseudomonas putida.
To investigate the copper-binding properties and redox activities of this unique fusion protein.
To elucidate the structural determinants differentiating tight-affinity versus weak-affinity copper binding in Sco proteins.

Main Methods:

X-ray crystallography for structural characterization.
Biochemical assays to assess copper binding affinity and redox activity.
Comparative structural analysis of bacterial and eukaryotic Sco domains.

Main Results:

The Pseudomonas putida Sco domain binds copper(I) weakly without involving the conserved histidine.
This Sco domain exhibits thioredoxin activity and can reduce Cu(II) to Cu(I) and Fe(III) to Fe(II).
Structural comparisons identified key differences influencing copper binding affinity.

Conclusions:

Histidine coordination is a critical factor differentiating metallochaperone versus redox functions in Sco proteins.
The fusion of Sco domain with cytochrome c in P. putida results in a protein with distinct copper-binding and redox properties.
Structural insights explain the variation in copper-binding affinity across different Sco proteins.