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      Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx

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          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 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 ~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.

          Abstract

          Significant challenges exist for structural characterization of enzymes responsible for biomineralization. Here the authors show that native mass spectrometry and high resolution electron microscopy can define the subunit topology and copper binding of a manganese oxidizing complex, and describe early stage formation of its mineral products

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          Most cited references 62

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          NIH Image to ImageJ: 25 years of image analysis.

          For the past 25 years NIH Image and ImageJ software have been pioneers as open tools for the analysis of scientific images. We discuss the origins, challenges and solutions of these two programs, and how their history can serve to advise and inform other software projects.
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            The I-TASSER Suite: protein structure and function prediction.

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              Multicopper Oxidases and Oxygenases.

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                Author and article information

                Contributors
                romano.christine@gmail.com
                mowei.zhou2012@gmail.com
                tebob@ohsu.edu
                Journal
                Nat Commun
                Nat Commun
                Nature Communications
                Nature Publishing Group UK (London )
                2041-1723
                29 September 2017
                29 September 2017
                2017
                : 8
                Affiliations
                [1 ]ISNI 0000 0000 9758 5690, GRID grid.5288.7, Institute of Environmental Health, , Oregon Health & Science University, ; 3181 SW Sam Jackson Park Road, Portland, OR 97239 USA
                [2 ]ISNI 0000 0001 2218 3491, GRID grid.451303.0, Environmental Molecular Sciences Laboratory, , Pacific Northwest National Laboratory, ; 3335 Innovation Blvd, Richland, WA 99354 USA
                [3 ]ISNI 0000 0001 2285 7943, GRID grid.261331.4, Department of Chemistry and Biochemistry, , Ohio State University, ; 460W 12th Ave, Columbus, OH 43210 USA
                Article
                896
                10.1038/s41467-017-00896-8
                5622069
                28963463
                © The Author(s) 2017

                Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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