Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx
Abstract
Bacteria that produce Mn oxides are extraordinarily skilled engineers of nanomaterials that contribute significantly to global biogeochemical cycles. Their enzyme-based reaction mechanisms may be genetically tailored for environmental remediation applications or bioenergy production. However, significant challenges exist for structural characterization of the enzymes responsible for biomineralization. The active Mn oxidase, Mnx, in Bacillus sp. PL-12 is a complex composed of a multicopper oxidase (MCO), MnxG, and two accessory proteins MnxE and MnxF. MnxG shares sequence similarity with other, structurally characterized MCOs. However, MnxE and MnxF have no similarity to any characterized proteins. The ~200 kDa complex has been recalcitrant to crystallization, so its structure is unknown. In this study, native mass spectrometry defines the subunit topology and copper binding of the Mnx complex, while high resolution electron microscopy visualizes the protein and nascent Mn oxide minerals. Furthermore, these data provide critical structural information for conceptualizing how Mnx produces nanoparticulate Mn oxides.
- Authors:
-
- Oregon Health & Science Univ., Portland, OR (United States)
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
- The Ohio State Univ., Columbus, OH (United States)
- Publication Date:
- Research Org.:
- Pacific Northwest National Laboratory (PNNL), Richland, WA (United States). Environmental Molecular Sciences Laboratory (EMSL)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1406743
- Report Number(s):
- PNNL-SA-124759
Journal ID: ISSN 2041-1723; 48903; KP1704020
- Grant/Contract Number:
- AC05-76RL01830
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 8; Journal Issue: 1; Journal ID: ISSN 2041-1723
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Environmental Molecular Sciences Laboratory
Citation Formats
Romano, Christine A., Zhou, Mowei, Song, Yang, Wysocki, Vicki H., Dohnalkova, Alice C., Kovarik, Libor, Pasa-Tolic, Ljiljana, and Tebo, Bradley M. Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx. United States: N. p., 2017.
Web. doi:10.1038/s41467-017-00896-8.
Romano, Christine A., Zhou, Mowei, Song, Yang, Wysocki, Vicki H., Dohnalkova, Alice C., Kovarik, Libor, Pasa-Tolic, Ljiljana, & Tebo, Bradley M. Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx. United States. https://doi.org/10.1038/s41467-017-00896-8
Romano, Christine A., Zhou, Mowei, Song, Yang, Wysocki, Vicki H., Dohnalkova, Alice C., Kovarik, Libor, Pasa-Tolic, Ljiljana, and Tebo, Bradley M. Fri .
"Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx". United States. https://doi.org/10.1038/s41467-017-00896-8. https://www.osti.gov/servlets/purl/1406743.
@article{osti_1406743,
title = {Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx},
author = {Romano, Christine A. and Zhou, Mowei and Song, Yang and Wysocki, Vicki H. and Dohnalkova, Alice C. and Kovarik, Libor and Pasa-Tolic, Ljiljana and Tebo, Bradley M.},
abstractNote = {Bacteria that produce Mn oxides are extraordinarily skilled engineers of nanomaterials that contribute significantly to global biogeochemical cycles. Their enzyme-based reaction mechanisms may be genetically tailored for environmental remediation applications or bioenergy production. However, significant challenges exist for structural characterization of the enzymes responsible for biomineralization. The active Mn oxidase, Mnx, in Bacillus sp. PL-12 is a complex composed of a multicopper oxidase (MCO), MnxG, and two accessory proteins MnxE and MnxF. MnxG shares sequence similarity with other, structurally characterized MCOs. However, MnxE and MnxF have no similarity to any characterized proteins. The ~200 kDa complex has been recalcitrant to crystallization, so its structure is unknown. In this study, native mass spectrometry defines the subunit topology and copper binding of the Mnx complex, while high resolution electron microscopy visualizes the protein and nascent Mn oxide minerals. Furthermore, these data provide critical structural information for conceptualizing how Mnx produces nanoparticulate Mn oxides.},
doi = {10.1038/s41467-017-00896-8},
journal = {Nature Communications},
number = 1,
volume = 8,
place = {United States},
year = {Fri Sep 29 00:00:00 EDT 2017},
month = {Fri Sep 29 00:00:00 EDT 2017}
}
Web of Science
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