ArticleApplied and environmental microbiology2014
Heterologous expression and characterization of the manganese-oxidizing protein from Erythrobacter sp. strain SD21.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 48 citations in OpenAlex.
- Advances in Research on Bacterial Oxidation of Mn(II): A Visualized Bibliometric Analysis Based on CiteSpace.Microorganisms · 2024Review
- A soil-borne Mn(II)-oxidizing bacterium of Providencia sp. exploits a strategy of superoxide production coupled to hydrogen peroxide consumption to generate Mn oxides.Archives of microbiology · 2022Article
- Article
- A novel bacterial thiosulfate oxidation pathway provides a new clue about the formation of zero-valent sulfur in deep sea.The ISME journal · 2020Article
- MopA, the Mn Oxidizing Protein FromFrontiers in microbiology · 2018Article
- Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx.Nature communications · 2017Article
- Identification of a Third Mn(II) Oxidase Enzyme in Pseudomonas putida GB-1.Applied and environmental microbiology · 2016Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
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Abstract
The manganese (Mn)-oxidizing protein (MopA) from Erythrobacter sp. strain SD21 is part of a unique enzymatic family that is capable of oxidizing soluble Mn(II). This enzyme contains two domains, an animal heme peroxidase domain, which contains the catalytic site, followed by a C-terminal calcium binding domain. Different from the bacterial Mn-oxidizing multicopper oxidase enzymes, little is known about MopA. To gain a better understanding of MopA and its role in Mn(II) oxidation, the 238-kDa full-length protein and a 105-kDa truncated protein containing only the animal heme peroxidase domain were cloned and heterologously expressed in Escherichia coli. Despite having sequence similarity to a peroxidase, hydrogen peroxide did not stimulate activity, nor was activity significantly decreased in the presence of catalase. Both pyrroloquinoline quinone (PQQ) and hemin increased Mn-oxidizing activity, and calcium was required. The Km for Mn(II) of the full-length protein in cell extract was similar to that of the natively expressed protein, but the Km value for the truncated protein in cell extract was approximately 6-fold higher than that of the full-length protein, suggesting that the calcium binding domain may aid in binding Mn(II). Characterization of the heterologously expressed MopA has provided additional insight into the mechanism of bacterial Mn(II) oxidation, which will aid in understanding the role of MopA and Mn oxidation in bioremediation and biogeochemical cycling.
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