Editing Extremophile (section)

=== Metals ===
''[[Acidithiubacillus ferroxidans]]'' has been shown to be effective in remediating mercury in acidic soil due to its ''merA'' gene making it mercury resistant.<ref>{{Cite journal |last1=Takeuchi |first1=Fumiaki |last2=Iwahori |first2=Kenji |last3=Kamimura |first3=Kazuo |last4=Negishi |first4=Atsunori |last5=Maeda |first5=Terunobu |last6=Sugio |first6=Tsuyoshi |date=January 2001 |title=Volatilization of Mercury under Acidic Conditions from Mercury-polluted Soil by a Mercury-resistant Acidithiobacillus ferrooxidans SUG 2-2 |journal=Bioscience, Biotechnology, and Biochemistry |volume=65 |issue=9 |pages=1981–86 |doi=10.1271/bbb.65.1981 |issn=0916-8451 |pmid=11676009 |s2cid=2158906|doi-access=free }}</ref> Industrial effluent contain high levels of metals that can be detrimental to both human and ecosystem health.<ref>{{Cite journal |last=Nagajyoti |first=P.C. |date=2008 |title=Heavy metal toxicity: Industrial Effluent Effect on Groundnut (Arachis hypogaea L.) Seedlings |journal=Journal of Applied Sciences Research |volume=4 |issue=1 |pages=110–21}}</ref><ref>{{Cite journal |last=Fakayode |first=S.O. |date=2005 |title=Impact assessment of industrial effluent on water quality of the receiving Alaro River in Ibadan, Nigeria. |journal=African Journal of Environmental Assessment and Management |volume=10 |pages=1–13}}</ref> In extreme heat environments the extremophile ''[[Geobacillus thermodenitrificans]]'' has been shown to effectively manage the concentration of these metals within twelve hours of introduction.<ref>{{Cite journal |last1=Chatterjee |first1=S.K. |last2=Bhattacharjee |first2=I. |last3=Chandra |first3=G. |date=March 2010 |title=Biosorption of heavy metals from industrial waste water by Geobacillus thermodenitrificans |journal=Journal of Hazardous Materials |volume=175 |issue=1–3 |pages=117–25 |doi=10.1016/j.jhazmat.2009.09.136 |issn=0304-3894 |pmid=19864059}}</ref> Some acidophilic microorganisms are effective at metal remediation in acidic environments due to proteins found in their periplasm, not present in any mesophilic organisms, allowing them to protect themselves from high proton concentrations.<ref>{{Cite journal |last=Chi |first=A. |date=2007 |title=Periplasmic proteins of the extremophile Acidithiobacillus ferrooxidans: a high throughput proteomics analysis |journal=Molecular & Cellular Proteomics |volume=6 |issue=12 |pages=2239–51 |doi=10.1074/mcp.M700042-MCP200  |doi-access=free |pmc=4631397 |pmid=17911085}}</ref> [[Paddy field|Rice paddies]] are highly oxidative environments that can produce high levels of lead or cadmium. ''[[Deinococcus radiodurans]]'' are resistant to the harsh conditions of the environment and are therefore candidate species for limiting the extent of contamination of these metals.<ref>{{Cite journal |last1=Dai |first1=Shang |last2=Chen |first2=Qi |last3=Jiang |first3=Meng |last4=Wang |first4=Binqiang |last5=Xie |first5=Zhenming |last6=Yu |first6=Ning |last7=Zhou |first7=Yulong |last8=Li |first8=Shan |last9=Wang |first9=Liangyan |last10=Hua |first10=Yuejin |last11=Tian |first11=Bing |date=September 2021 |title=Colonized extremophile Deinococcus radiodurans alleviates toxicity of cadmium and lead by suppressing heavy metal accumulation and improving antioxidant system in rice |journal=Environmental Pollution |volume=284 |pages=117127 |doi=10.1016/j.envpol.2021.117127 |issn=0269-7491 |pmid=33892465|bibcode=2021EPoll.28417127D }}</ref>

Some bacteria are known to also use [[Rare-earth element|rare earth elements]] on their biological processes. For example, ''[[Methylacidiphilum fumariolicum]]'', ''[[Methylorubrum extorquens]],'' and ''[[Methylobacterium radiotolerans]]'' are known to be able to use [[Lanthanide#Biological effects|lanthanides]] as cofactors to increase their [[methanol dehydrogenase]] activity.<ref>{{Cite journal |last1=Phi |first1=Manh Tri |last2=Singer |first2=Helena |last3=Zäh |first3=Felix |last4=Haisch |first4=Christoph |last5=Schneider |first5=Sabine |last6=Op den Camp |first6=Huub J. M. |last7=Daumann |first7=Lena J. |date=2024-03-01 |title=Assessing Lanthanide-Dependent Methanol Dehydrogenase Activity: The Assay Matters |url=https://pubmed.ncbi.nlm.nih.gov/38269599/ |journal=ChemBioChem |volume=25 |issue=5 |pages=e202300811 |doi=10.1002/cbic.202300811 |issn=1439-7633 |pmid=38269599}}</ref><ref>{{Citation |last1=Good |first1=Nathan M. |date=2021-01-01 |volume=650 |pages=97–118 |editor-last=Cotruvo |editor-first=Joseph A. |url=https://www.sciencedirect.com/science/article/pii/S0076687921000719 |access-date=2024-04-10  |publisher=Academic Press |last2=Martinez-Gomez |first2=N. Cecilia|title=Rare-Earth Element Biochemistry: Methanol Dehydrogenases and Lanthanide Biology |chapter=Expression, purification and testing of lanthanide-dependent enzymes in Methylorubrum extorquens AM1 |series=Methods in Enzymology |doi=10.1016/bs.mie.2021.02.001 |pmid=33867027 |isbn=978-0-12-823856-1 }}</ref>{{citation needed|date=May 2023}}