Kinetics of Mn(II) oxidation by Leptothrix discophora SS1

Zhang, Jinghao; Lion, Leonard W.; Nelson, Yarrow M.; Shuler, Michael L.; Ghiorse, William C.

doi:10.1016/s0016-7037(01)00808-0

Cited by 103 publications

(66 citation statements)

References 25 publications

(22 reference statements)

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“…SD21. This stimulation has been shown in other Mn(II)-oxidizing bacteria (van Waasbergen et al 1996;Larsen et al 1999;Brouwers et al 2000a;Zhang et al 2002). With growing whole cells of Erythrobacter sp.…”

Section: Optimization Of the Mn(ii) Oxidase Assay And Identification mentioning

confidence: 54%

“…The absorbance spectra of the partially purified activity does not show characteristics consistent with an MCO, and copper does not affect Mn (II) oxidation by Erythrobacter sp. SD21 in vivo or in vitro as has been shown in other Mn (II)-oxidizing microorganisms (van Waasbergen et al 1996;Larsen et al 1999;Brouwers et al 2000a;Zhang et al 2002). In addition, in contrast to what has been observed with other Mn (II)-oxidizing protein preparations (Webb et al 2004), Mn(III) instead of Mn(IV) seems to be the product of Mn(II) oxidation; thus, a different catalytic mechanism may be employed.…”

Section: Discussionmentioning

confidence: 92%

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In vitro studies indicate a quinone is involved in bacterial Mn(II) oxidation

Johnson

Tebo

2007

Arch Microbiol

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Manganese(II)-oxidizing bacteria play an integral role in the cycling of Mn as well as other metals and organics. Prior work with Mn(II)-oxidizing bacteria suggested that Mn(II) oxidation involves a multicopper oxidase, but whether this enzyme directly catalyzes Mn(II) oxidation is unknown. For a clearer understanding of Mn(II) oxidation, we have undertaken biochemical studies in the model marine α-proteobacterium, Erythrobacter sp. strain SD21. The optimum pH for Mn(II)-oxidizing activity was 8.0 with a specific activity of 2.5 nmol × min −1 × mg −1 and a K m = 204 µM. The activity was soluble suggesting a cytoplasmic or periplasmic protein. Mn(III) was an intermediate in the oxidation of Mn(II) and likely the primary product of enzymatic oxidation. The activity was stimulated by pyrroloquinoline quinone (PQQ), NAD + , and calcium but not by copper. In addition, PQQ rescued Pseudomonas putida MnB1 non Mn(II)-oxidizing mutants with insertions in the anthranilate synthase gene. The substrate and product of anthranilate synthase are intermediates in various quinone biosyntheses. Partially purified Mn(II) oxidase was enriched in quinones and had a UV/VIS absorption spectrum similar to a known quinone requiring enzyme but not to multicopper oxidases. These studies suggest that quinones may play an integral role in bacterial Mn(II) oxidation.

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Section: Optimization Of the Mn(ii) Oxidase Assay And Identification mentioning

confidence: 54%

Section: Discussionmentioning

confidence: 92%

In vitro studies indicate a quinone is involved in bacterial Mn(II) oxidation

Johnson

Tebo

2007

Arch Microbiol

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“…However, the role of mofA in enzymatic Mn(II) oxidation in L. discophora SS-1 has never been unequivocally determined because of the recalcitrance of Leptothrix to genetic manipulation. Despite the fact that the involvement of multicopper oxidases seems to be a common feature of microbial manganese oxidation (7,19,33,43), no bacterial Mn(II) oxidase has been purified in quantities sufficient for detailed biochemical study. In addition, no multicopper oxidase gene thought to encode a Mn(II) oxidase has ever conferred heterologous expression of an active Mn(II)-oxidizing enzyme (5,40).…”

Section: Discussionmentioning

confidence: 99%

“…Experiments were performed in 2-liter magnetically stirred jacketed vessels at temperatures of 25 to 27°C (43). The working volume in each reactor was 25%.…”

Section: Methodsmentioning

confidence: 99%

Iron Requirement for Mn(II) Oxidation by Leptothrix discophora SS-1

Gheriany¹,

Bocioaga²,

Hay³

et al. 2009

Appl Environ Microbiol

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The biological catalysis of Mn(II) oxidation is thought to be responsible for the formation of most naturally occurring insoluble Mn(III, IV) oxides (40, 41) and consequently plays a key role in the biogeochemical cycling of Mn. The resulting biogenic Mn oxides have high adsorptive capacities for toxic metals (16, 17) and can oxidize both natural organic compounds (38) and organic contaminants (36). The binding of transition metals to biogenic Mn oxides can, in turn, greatly affect the phase distributions and residence times of these transition metals in many natural systems (16,17). An understanding of environmental conditions that favor or inhibit the production of the extracellular enzyme responsible for Mn(II) oxidation will contribute to insight into this important ecological process and is also a prerequisite for the design of any successful technology that uses microorganisms for the production of Mn oxides.A variety of phylogenetically distinct microorganisms are capable of the extracellular oxidation of Mn(II) (5). Based on the presence of conserved predicted amino acid motifs, the genes that encode putative Mn(II)-oxidizing enzymes (mofA in Leptothrix discophora [9], cumA in Pseudomonas putida GB-1 [7], and moxA in Pedomicrobium sp. strain ACM 3067 [33]) are all thought to produce multicopper oxidases. Recently, further support for the role of putative multicopper oxidases in Mn(II) oxidation has come from the recovery and sequencing of peptides excised from Mn(II)-oxidizing bands in polyacrylamide gel analyses of proteins from three Mn(II)-oxidizing Bacillus species (15). Specifically, Mn(II)-oxidizing bands from the exosporia of two of the three Bacillus species tested were shown by tandem mass spectrometric analyses to contain peptides with homology to the predicted C terminus of the putative multicopper Mn(II) oxidase MnxG.Despite this growing body of evidence regarding the role of multicopper oxidases in Mn(II) oxidation, little is known about how the concentrations of different nutrients (e.g., iron, carbon, and nitrogen) or growth conditions such as pH and the oxygen concentration regulate the production of the enzyme(s) which oxidizes Mn(II). Nelson et al. (26) evaluated the minimal growth conditions needed for Mn(II) oxidation and found that the addition of 0.1 M Fe(II) to the defined minimal mineral salt (MMS) medium used for growth was necessary for the complete oxidation of Mn(II) by L. discophora SS-1; however, adding 0.1 M Fe(II) to stationary-phase cells did not allow complete Mn(II) oxidation.In the present study, we grew L. discophora SS-1 in a controlled-reactor system and evaluated the time courses of Mn(II) oxidation and mofA transcript levels in batch cultures of cells with limited and sufficient iron. Parker et al. (30) observed that retarded Mn(IV) formation by iron-starved P. putida is a consequence of the binding of the Mn(III) intermediate (42) to the siderophore pyoverdine. Therefore, siderophore production was also evaluated as part of this research. MATERIALS AND METHODS...

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“…These biogenic Mn oxides exhibited specific surface areas and toxic metal adsorption capacities that were significantly greater than that of abiotic Mn oxides (Figure 1 and Nelson, et al 1999). The author has subsequently measured biological Mn oxidation kinetics (Zhang et al 2002) and examined toxic metal adsorption to mixtures of Mn and Fe oxides . However, what remains to be done is to prove the application of this technology for the treatment of metal-contaminated wastewaters.…”

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confidence: 99%

The California Central Coast Research Partnership: Building Relationships, Partnerships and Paradigms for University-Industry Research Collaboration (Abridged Version)

Opava¹

2004

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Kinetics of Mn(II) oxidation by Leptothrix discophora SS1

Cited by 103 publications

References 25 publications

In vitro studies indicate a quinone is involved in bacterial Mn(II) oxidation

In vitro studies indicate a quinone is involved in bacterial Mn(II) oxidation

Iron Requirement for Mn(II) Oxidation by Leptothrix discophora SS-1

The California Central Coast Research Partnership: Building Relationships, Partnerships and Paradigms for University-Industry Research Collaboration (Abridged Version)

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