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.
Original language | English |
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Pages (from-to) | 1886-1890 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 588 |
Issue number | 10 |
DOIs | |
State | Published - May 21 2014 |
Funding
DJR is a Royal Society Wolfson Foundation Merit Award holder. This research was supported by the Biotechnology and Biological Sciences Research Council ( BB/K00929X/1 and BB/H007288/1 ) and sponsored by the Subsurface Biogeochemical Research program (SBR)/Office of Biological and Environmental Research (BER) , U.S. Department of Energy (DOE) , and is a contribution of the Pacific Northwest National Laboratory (PNNL) Scientific Focus Area and the Mercury Scientific Focus Area at Oak Ridge National Laboratory (ORNL). The PNNL and ORNL are operated for the DOE by Battelle under contracts DE-AC05-76RLO1830 and DE-AC05-00OR22725
Funders | Funder number |
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U.S. Department of Energy | |
Biological and Environmental Research | |
Oak Ridge National Laboratory | |
Pacific Northwest National Laboratory | |
Biotechnology and Biological Sciences Research Council | BB/H007288/1, BB/K00929X/1 |
Keywords
- Electron transfer
- Metalloprotein
- Mineral respiration
- Multiheme cytochrome
- Outer membrane
- Shewanella
- c-Type heme