Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx

Christine A. Romano, Mowei Zhou, Yang Song, Vicki H. Wysocki, Alice C. Dohnalkova, Libor Kovarik, Ljiljana Paša-Tolić, Bradley Tebo

Research output: Contribution to journalArticle

16 Citations (Scopus)

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.

Original languageEnglish (US)
Article number746
JournalNature Communications
Volume8
Issue number1
DOIs
StatePublished - Dec 1 2017

Fingerprint

manganese oxides
oxidase
Nanoparticles
Biomineralization
enzymes
Oxidoreductases
proteins
nanoparticles
Oxides
Enzymes
Oxide minerals
Proteins
oxides
Nanostructures
accessories
Bacillus
High resolution electron microscopy
Accessories
Bacilli
Crystallization

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

Cite this

Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx. / Romano, Christine A.; Zhou, Mowei; Song, Yang; Wysocki, Vicki H.; Dohnalkova, Alice C.; Kovarik, Libor; Paša-Tolić, Ljiljana; Tebo, Bradley.

In: Nature Communications, Vol. 8, No. 1, 746, 01.12.2017.

Research output: Contribution to journalArticle

Romano, CA, Zhou, M, Song, Y, Wysocki, VH, Dohnalkova, AC, Kovarik, L, Paša-Tolić, L & Tebo, B 2017, 'Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx', Nature Communications, vol. 8, no. 1, 746. https://doi.org/10.1038/s41467-017-00896-8
Romano, Christine A. ; Zhou, Mowei ; Song, Yang ; Wysocki, Vicki H. ; Dohnalkova, Alice C. ; Kovarik, Libor ; Paša-Tolić, Ljiljana ; Tebo, Bradley. / Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx. In: Nature Communications. 2017 ; Vol. 8, No. 1.
@article{e2dab61ab69841058893d9b1c7b8b681,
title = "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 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.",
author = "Romano, {Christine A.} and Mowei Zhou and Yang Song and Wysocki, {Vicki H.} and Dohnalkova, {Alice C.} and Libor Kovarik and Ljiljana Paša-Tolić and Bradley Tebo",
year = "2017",
month = "12",
day = "1",
doi = "10.1038/s41467-017-00896-8",
language = "English (US)",
volume = "8",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",
number = "1",

}

TY - JOUR

T1 - Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx

AU - Romano, Christine A.

AU - Zhou, Mowei

AU - Song, Yang

AU - Wysocki, Vicki H.

AU - Dohnalkova, Alice C.

AU - Kovarik, Libor

AU - Paša-Tolić, Ljiljana

AU - Tebo, Bradley

PY - 2017/12/1

Y1 - 2017/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85030310144&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85030310144&partnerID=8YFLogxK

U2 - 10.1038/s41467-017-00896-8

DO - 10.1038/s41467-017-00896-8

M3 - Article

VL - 8

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 746

ER -