Journal
NATURE COMMUNICATIONS
Volume 8, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-017-00896-8
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Funding
- National Science Foundation [CHE-1410688]
- National Institute of Health [NIH R01GM113658]
- NSF [DBI-1202859]
- Environmental and Molecular Sciences Laboratory (EMSL), a DOE Office of Science User Facility - Office of Biological and Environmental Research
- Division Of Chemistry [1410688] Funding Source: National Science Foundation
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM113658] Funding Source: NIH RePORTER
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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 in Bacillus sp. PL-12, Mnx, 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. MnxE and MnxF have no similarity to any characterized proteins. The similar to 200 kDa complex has been recalcitrant to crystallization, so its structure is unknown. Here, we show that native mass spectrometry defines the subunit topology and copper binding of Mnx, while high-resolution electron microscopy visualizes the protein and nascent Mn oxide minerals. These data provide critical structural information for understanding Mn biomineralization by such unexplored enzymes.
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