Mn(II) Oxidation Is Catalyzed by Heme Peroxidases in “
            <i>Aurantimonas manganoxydans</i>
            ” Strain SI85-9A1 and
            <i>Erythrobacter</i>
            sp. Strain SD-21

Anderson, Craig; Johnson, Hope A.; Caputo, Nicholas; Davis, R. E.; Torpey, Justin W.; Tebo, Bradley M.

doi:10.1128/aem.02890-08

Cited by 122 publications

(135 citation statements)

References 49 publications

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“…However, several genes showed a markedly higher transcript abundance in the plume environment, including an MGI archaea ammonium transporter (8.6 times increase) and SUP05 genes for the sox sulfur oxidation system (10-20 times increase) (Figure 2). Notably absent from the abundant protein-coding transcripts were genes encoding known Mn-oxidizing enzymes such as the multicopper oxidases MnxG, CumA and MofA (for example, Dick et al, 2008b) or the heme peroxidase MopA (for example, Dick et al, 2008a;Anderson et al, 2009). Although expression of novel multicopper oxidases was observed (mRNA transcript abundance ranks 186, 282, 818 and 856; data not shown in Figure 2), this diverse family of enzymes oxidizes a wide range of substrates (Tebo et al, 2004), thus further investigation is required to evaluate their potential link to Mn oxidation.…”

Section: Resultsmentioning

confidence: 99%

The metatranscriptome of a deep-sea hydrothermal plume is dominated by water column methanotrophs and lithotrophs

et al. 2012

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Microorganisms mediate geochemical processes in deep-sea hydrothermal vent plumes, which are a conduit for transfer of elements and energy from the subsurface to the oceans. Despite this important microbial influence on marine geochemistry, the ecology and activity of microbial communities in hydrothermal plumes is largely unexplored. Here, we use a coordinated metagenomic and metatranscriptomic approach to compare microbial communities in Guaymas Basin hydrothermal plumes to background waters above the plume and in the adjacent Carmen Basin. Despite marked increases in plume total RNA concentrations (3-4 times) and microbially mediated manganese oxidation rates (15-125 times), plume and background metatranscriptomes were dominated by the same groups of methanotrophs and chemolithoautotrophs. Abundant community members of Guaymas Basin seafloor environments (hydrothermal sediments and chimneys) were not prevalent in the plume metatranscriptome. De novo metagenomic assembly was used to reconstruct genomes of abundant populations, including Marine Group I archaea, Methylococcaceae, SAR324 Deltaproteobacteria and SUP05 Gammaproteobacteria. Mapping transcripts to these genomes revealed abundant expression of genes involved in the chemolithotrophic oxidation of ammonia (amo), methane (pmo) and sulfur (sox). Whereas amo and pmo gene transcripts were abundant in both plume and background, transcripts of sox genes for sulfur oxidation from SUP05 groups displayed a 10-20-fold increase in plumes. We conclude that the biogeochemistry of Guaymas Basin hydrothermal plumes is mediated by microorganisms that are derived from seawater rather than from seafloor hydrothermal environments such as chimneys or sediments, and that hydrothermal inputs serve as important electron donors for primary production in the deep Gulf of California.

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Section: Resultsmentioning

confidence: 99%

The metatranscriptome of a deep-sea hydrothermal plume is dominated by water column methanotrophs and lithotrophs

et al. 2012

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“…The Mn(II) oxidase enzymes that have been identified so far are found loosely bound to the exosporium (40) or the outer membrane (15) or are secreted from the cell into the culture milieu (17). P. putida GB-1 MopA is secreted into the culture supernatant (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…SD-21, and Roseobacter sp. AzwK-3b (15)(16)(17). However, deletion of this gene (mopA) from the P. putida GB-1 genome had little reproducible effect on Mn(II) oxidation.…”

Section: Table 2 Primers Used In This Studymentioning

confidence: 99%

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Identification of a Third Mn(II) Oxidase Enzyme in Pseudomonas putida GB-1

Geszvain

Smesrud

Tebo

2016

Appl Environ Microbiol

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The oxidation of soluble Mn(II) to insoluble Mn(IV) is a widespread bacterial activity found in a diverse array of microbes. In the Mn(II)-oxidizing bacterium Pseudomonas putida GB-1, two Mn(II) oxidase genes, named mnxG and mcoA, were previously identified; each encodes a multicopper oxidase (MCO)-type enzyme. Expression of these two genes is positively regulated by the response regulator MnxR. Preliminary investigation into putative additional regulatory pathways suggested that the flagellar regulators FleN and FleQ also regulate Mn(II) oxidase activity; however, it also revealed the presence of a third, previously uncharacterized Mn(II) oxidase activity in P. putida GB-1. A strain from which both of the Mn(II) oxidase genes and fleQ were deleted exhibited low levels of Mn(II) oxidase activity. The enzyme responsible was genetically and biochemically identified as an animal heme peroxidase (AHP) with domain and sequence similarity to the previously identified Mn(II) oxidase MopA. In the ⌬fleQ strain, P. putida GB-1 MopA is overexpressed and secreted from the cell, where it actively oxidizes Mn. Thus, deletion of fleQ unmasked a third Mn(II) oxidase activity in this strain. These results provide an example of an Mn(II)-oxidizing bacterium utilizing both MCO and AHP enzymes. IMPORTANCEThe identity of the Mn(II) oxidase enzyme in Pseudomonas putida GB-1 has been a long-standing question in the field of bacterial Mn(II) oxidation. In the current work, we demonstrate that P. putida GB-1 employs both the multicopper oxidase-and animal heme peroxidase-mediated pathways for the oxidation of Mn(II), rendering this model organism relevant to the study of both types of Mn(II) oxidase enzymes. The presence of three oxidase enzymes in P. putida GB-1 deepens the mystery of why microorganisms oxidize Mn(II) while providing the field with the tools necessary to address this question. The initial identification of MopA as a Mn(II) oxidase in this strain required the deletion of FleQ, a regulator involved in both flagellum synthesis and biofilm synthesis in Pseudomonas aeruginosa. Therefore, these results are also an important step toward understanding the regulation of Mn(II) oxidation.

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“…Whereas the bacteria Aurantimonas maganoxydans SI85-9A1 and Erythrobacter sp. strain SD-21 are thought to use a manganese-oxidizing peroxidase (Anderson et al 2009). Similarly, fungi of the Basidiomycetes are known to use a manganese peroxidase enzyme (Liers et al 2011) to oxidize Mn (II).…”

Section: Sustained Anthropogenic Impact In Carter Saltpeter Cave Carmentioning

confidence: 99%

Sustained Anthropogenic Impact in Carter Saltpeter Cave, Carter County, Tennessee and the Potential Effects on Manganese Cycling

Carmichael¹,

Carmichael²,

Strom³

et al. 2013

JCKS

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Mn(II) Oxidation Is Catalyzed by Heme Peroxidases in “ Aurantimonas manganoxydans ” Strain SI85-9A1 and Erythrobacter sp. Strain SD-21

Cited by 122 publications

References 49 publications

The metatranscriptome of a deep-sea hydrothermal plume is dominated by water column methanotrophs and lithotrophs

The metatranscriptome of a deep-sea hydrothermal plume is dominated by water column methanotrophs and lithotrophs

Identification of a Third Mn(II) Oxidase Enzyme in Pseudomonas putida GB-1

Sustained Anthropogenic Impact in Carter Saltpeter Cave, Carter County, Tennessee and the Potential Effects on Manganese Cycling

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