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Updated: May 1, 2026

In Situ Characterization of Shewanella oneidensis MR1 Biofilms by SALVI and ToF-SIMS
Published on: August 18, 2017
The X-ray crystal structure of Shewanella oneidensis OmcA reveals new insight at the microbe-mineral interface
Marcus J Edwards1, Nanakow A Baiden1, Alexander Johs2
1Centre for Molecular and Structural Biochemistry, School of Biological Sciences and School of Chemistry, University of East Anglia, Norwich NR4 7TJ, United Kingdom.
Abstract:
The X-ray crystal structure of Shewanella oneidensis OmcA, an extracellular decaheme cytochrome involved in mineral reduction, was solved to a resolution of 2.7 Å. The four OmcA molecules in the asymmetric unit are arranged so the minimum distance between heme 5 on adjacent OmcA monomers is 9 Å, indicative of a transient OmcA dimer capable of intermolecular electron transfer. A previously identified hematite binding motif was identified near heme 10, forming a hydroxylated surface that would bring a heme 10 electron egress site to ∼10 Å of a mineral surface.
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