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Limited role of sessile acidophiles in pyrite oxidation below redox potential of 650 mV.

ABSTRACT: Pyrite oxidation by mixed mesophilic acidophiles was conducted under conditions of controlled and non-controlled redox potential to investigate the role of sessile microbes in pyrite oxidation. Microbes attached on pyrite surfaces by extracellular polymeric substances (EPS), and their high coverage rate was characterized by scanning electron microscopy (SEM), confocal laser scanning microscopy (CLSM) and atomic force microscopy (AFM). The dissolution of pyrite was negligible if the redox potential was controlled below 650 mV (near the rest potential of pyrite), even though the bacteria were highly active and a high coverage rate was observed on pyrite surfaces. However, with un-controlled redox potential the rate of pyrite oxidation increased greatly with an increasing redox potential. This study demonstrates that sessile microbes play a limited role in pyrite oxidation at a redox potential below 650 mV, and highlight the importance of solution redox potential for pyrite oxidation. This has implications for acid mine drainage control and pyrite oxidation control in biometallurgy practice.

SUBMITTER: Liu C

PROVIDER: S-EPMC5504038 | biostudies-other | 2017 Jul

REPOSITORIES: biostudies-other

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Project description:The Rac1 GTPase is an essential and ubiquitous protein that signals through numerous pathways to control critical cellular processes, including cell growth, morphology, and motility. Rac1 deletion is embryonic lethal, and its dysregulation or mutation can promote cancer, arthritis, cardiovascular disease, and neurological disorders. Rac1 activity is highly regulated by modulatory proteins and posttranslational modifications. Whereas much attention has been devoted to guanine nucleotide exchange factors that act on Rac1 to promote GTP loading and Rac1 activation, cellular oxidants may also regulate Rac1 activation by promoting guanine nucleotide exchange. Herein, we show that Rac1 contains a redox-sensitive cysteine (Cys(18)) that can be selectively oxidized at physiological pH because of its lowered pKa. Consistent with these observations, we show that Rac1 is glutathiolated in primary chondrocytes. Oxidation of Cys(18) by glutathione greatly perturbs Rac1 guanine nucleotide binding and promotes nucleotide exchange. As aspartate substitutions have been previously used to mimic cysteine oxidation, we characterized the biochemical properties of Rac1(C18D). We also evaluated Rac1(C18S) as a redox-insensitive variant and found that it retains structural and biochemical properties similar to those of Rac1(WT) but is resistant to thiol oxidation. In addition, Rac1(C18D), but not Rac1(C18S), shows greatly enhanced nucleotide exchange, similar to that observed for Rac1 oxidation by glutathione. We employed Rac1(C18D) in cell-based studies to assess whether this fast-cycling variant, which mimics Rac1 oxidation by glutathione, affects Rac1 activity and function. Expression of Rac1(C18D) in Swiss 3T3 cells showed greatly enhanced GTP-bound Rac1 relative to Rac1(WT) and the redox-insensitive Rac1(C18S) variant. Moreover, expression of Rac1(C18D) in HEK-293T cells greatly promoted lamellipodia formation. Our results suggest that Rac1 oxidation at Cys(18) is a novel posttranslational modification that upregulates Rac1 activity.

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Limited role of sessile acidophiles in pyrite oxidation below redox potential of 650 mV.

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