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Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx
Christine A Romano1, Mowei Zhou2, Yang Song3
1Institute of Environmental Health, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, OR, 97239, USA. romano.christine@gmail.com.
Nature Communications
|October 1, 2017
Summary
Bacteria use manganese (Mn) oxidase enzymes to create nanomaterials. New techniques like native mass spectrometry and electron microscopy reveal the structure of these enzymes, aiding in environmental applications.
Area of Science:
- Biochemistry
- Microbiology
- Nanotechnology
Background:
- Bacteria producing manganese oxides are key players in global biogeochemical cycles.
- Their enzymes offer potential for environmental remediation and bioenergy.
- Structural characterization of biomineralization enzymes is challenging.
Purpose of the Study:
- To elucidate the structure of the Mnx manganese oxidase complex from Bacillus sp. PL-12.
- To understand the subunit topology and copper binding of the Mnx complex.
- To visualize the protein and early-stage mineral formation.
Main Methods:
- Native mass spectrometry was employed to determine subunit topology and copper binding.
- High-resolution electron microscopy was used to visualize the Mnx complex and nascent Mn oxide minerals.
Main Results:
- Native mass spectrometry successfully defined the subunit organization and copper coordination within the Mnx complex.
- Electron microscopy provided visual data on the protein structure and the initial stages of Mn oxide biomineralization.
- This study overcomes previous difficulties in crystallizing the ~200 kDa Mnx complex.
Conclusions:
- Native mass spectrometry and electron microscopy are powerful tools for characterizing complex biomineralization enzymes.
- The structural insights gained advance our understanding of manganese biomineralization.
- This knowledge can inform future bioengineering efforts for environmental and energy applications.
