Iron and sulfur oxidation pathways of Acidithiobacillus ferrooxidans

Zhan, Yue; Yang, Mengran; Zhang, Shuang; Zhao, Dan; Duan, Jiangong; Wang, Weidong; Yan, Lei

doi:10.1007/s11274-019-2632-y

Cited by 50 publications

(23 citation statements)

References 104 publications

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“…While the A. ferrooxidans gene model shows greater differences to our A. thiooxidans model, most notably in its absence of the Sox complex and sor gene, and its inclusion of SAT and TSD Zhan et al, 2019). For A. caldus and A. ferrooxidans, the current S 0 metabolism is proposed to be oxidation to SO 2− 3 via Sdo, followed by oxidation to SO 2− 4 via SAT, with the bacteria acquiring S 0 from extracellular sources (Mangold et al, 2011;Zhan et al, 2019). This differs to our proposed S 0 metabolic pathway (Figure 6A), which is elaborated upon further below.…”

Section: Comparisons To Previous Literaturementioning

confidence: 56%

“…Differing only that in A. caldus, Sdo has been determined to be located in the cytoplasm instead of the periplasm (Wu et al, 2017) and it has the addition of SAT responsible for oxidation of sulfite to sulfate . While the A. ferrooxidans gene model shows greater differences to our A. thiooxidans model, most notably in its absence of the Sox complex and sor gene, and its inclusion of SAT and TSD Zhan et al, 2019). For A. caldus and A. ferrooxidans, the current S 0 metabolism is proposed to be oxidation to SO 2− 3 via Sdo, followed by oxidation to SO 2− 4 via SAT, with the bacteria acquiring S 0 from extracellular sources (Mangold et al, 2011;Zhan et al, 2019).…”

Section: Comparisons To Previous Literaturementioning

confidence: 72%

“…Recent works reviewing Acidithiobacillus spp. sulfur metabolism have identified diverse pathways for this genus dependent on the species, as well as the sulfur substrate(s) (S 0 , S 2 O 2− 3 , S 4 O 2− 6 ) and the different sulfur metabolism genes available to them Zhan et al, 2019). These studies have provided updated models for A. caldus and A. ferrooxidans based on the existing literature of studies using either genomics, proteomics or sulfur chemistry analyses.…”

Section: Introductionmentioning

confidence: 99%

“…For both species, S 0 metabolism is proposed as oxidation to SO 2− 3 via Sdo, followed by oxidation to SO 2− 4 via the sulfate adenylyltransferase dissimilatory-type (SAT) gene . While the S 2 O 2− 3 metabolism is proposed to differ between the two species, where in A. caldus it is through the S 4 I pathway and Sox complex, and in A. ferrooxidans via the S 4 I pathway and thiosulfate dehydrogenase (TSD) Zhan et al, 2019). The S 4 I pathway utilizing the doxD (thiosulfate:quinone oxidoreductase) and tetH (tetrathionate hydrolase) genes .…”

Section: Introductionmentioning

confidence: 99%

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New Insights Into Acidithiobacillus thiooxidans Sulfur Metabolism Through Coupled Gene Expression, Solution Chemistry, Microscopy, and Spectroscopy Analyses

et al. 2020

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Here, we experimentally expand understanding of the reactions and enzymes involved in Acidithiobacillus thiooxidans ATCC 19377 S 0 and S 2 O 2− 3 metabolism by developing models that integrate gene expression analyzed by RNA-Seq, solution sulfur speciation, electron microscopy and spectroscopy. The A. thiooxidans S 2 O 2− 3 metabolism model involves the conversion of S 2 O 2− 3 to SO 2− 4 , S 0 and S 4 O 2− 6 , mediated by the sulfur oxidase complex (Sox), tetrathionate hydrolase (TetH), sulfide quinone reductase (Sqr), and heterodisulfate reductase (Hdr) proteins. These same proteins, with the addition of rhodanese (Rhd), were identified to convert S 0 to SO 2− 3 , S 2 O 2− 3 and polythionates in the A. thiooxidans S 0 metabolism model. Our combined results shed light onto the important role specifically of TetH in S 2 O 2− 3 metabolism. Also, we show that activity of Hdr proteins rather than Sdo are likely associated with S 0 oxidation. Finally, our data suggest that formation of intracellular S 2 O 2− 3 is a critical step in S 0 metabolism, and that recycling of internally generated SO 2− 3 occurs, through comproportionating reactions that result in S 2 O 2− 3 . Electron microscopy and spectroscopy confirmed intracellular production and storage of S 0 during growth on both S 0 and S 2 O 2− 3 substrates.

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Section: Comparisons To Previous Literaturementioning

confidence: 56%

Section: Comparisons To Previous Literaturementioning

confidence: 72%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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New Insights Into Acidithiobacillus thiooxidans Sulfur Metabolism Through Coupled Gene Expression, Solution Chemistry, Microscopy, and Spectroscopy Analyses

et al. 2020

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“…ferroxidans with a release of sulphate up to 8% w/w over 20 days; this result is more e cient when comparing with Thiobacillus thioparus and Acidianus brierleyi, under the same treatment conditions [13]. It is known that A. ferrooxidans can couple sulfur oxidation with electron transfer with a high redox potential for CO 2 xation, releasing sulfate ions at the end of the oxidation process [29].…”

Section: Sulfate Ion Quanti Cationmentioning

confidence: 99%

Desulfurization of Vulcanized Rubber Particles Using Biological and Chemical Methods

Valdés¹,

Hernández²,

Morales-Vera³

et al. 2020

Preprint

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Currently, recycling or degradation treatments for tires are an enormous challenge. Despite efforts to dispose of or recycle it, rubber waste is increasing year by year worldwide. To create a rubber-recycling system, several researchers have proposed tire desulfurization. In this study, we compare two methods: one biological, using Acidobacillus ferroxidans in shake 250 mL flask experiments, and one chemical using, for the first time, microwaves and an aqueous solution. The results of these methods were analyzed through sulfate quantification, cross-linking differences, Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy with energy disperse spectroscopy (SEM-EDS). We observed that the amount of sulfates generated by the chemical system was 56 mg / L, which was 10-times higher than the biological system, which generated 5.3 mg / L. Similarly, after cross-linking studies, a 36% higher decrease after the chemical treatment was observed. When using FTIR analysis, the disappearance of characteristic bands corresponding to functional groups containing sulfur bonds was observed by treating the sample with both desulfurization mechanisms. Morphological changes on the rubber surface structure was also demonstrated by SEM-EDS analysis with the appearance of holes, cracks and changes in the porosity of the material. This work analyzed two different non-aggressive desulfurization mechanisms that might be used as sustainable methods for rubber recycling processes.

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Enhanced microbial corrosion of stainless steel by Acidithiobacillus ferrooxidans through the manipulation of substrate oxidation and overexpression of rus

Inaba

West

Banta

2020

Biotech & Bioengineering

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Acidithiobacillus ferrooxidans cells can oxidize iron and sulfur and are key members of the microbial biomining communities that are exploited in the large-scale bioleaching of metal sulfide ores. Some minerals are recalcitrant to bioleaching due to the presence of other inhibitory materials in the ore bodies. Additives are intentionally included in processed metals to reduce environmental impacts and microbially influenced corrosion. We have previously reported a new aerobic corrosion

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Iron and sulfur oxidation pathways of Acidithiobacillus ferrooxidans

Cited by 50 publications

References 104 publications

New Insights Into Acidithiobacillus thiooxidans Sulfur Metabolism Through Coupled Gene Expression, Solution Chemistry, Microscopy, and Spectroscopy Analyses

New Insights Into Acidithiobacillus thiooxidans Sulfur Metabolism Through Coupled Gene Expression, Solution Chemistry, Microscopy, and Spectroscopy Analyses

Desulfurization of Vulcanized Rubber Particles Using Biological and Chemical Methods

Enhanced microbial corrosion of stainless steel by Acidithiobacillus ferrooxidans through the manipulation of substrate oxidation and overexpression of rus

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