Antimonite oxidation by microbial extracellular superoxide in

Antimony (Sb) is a re-emerging contaminant, and its redox transformation is mainly driven by microorganisms. Sb(III) oxidation has been attributed to enzymatic catalyzed reaction, though the physiological reason for this process remains unclear. Herein, we isolated a bacterium named Pseudomonas sp....
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Wang, Liying [verfasserIn] Ye, Li [verfasserIn] Yin, Zhipeng [verfasserIn] Zhang, Lixin [verfasserIn] Jing, Chuanyong [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Schlagwörter:	Antimonite oxidation Microbial extracellular superoxide Redox transformation

Übergeordnetes Werk:	Enthalten in: Geochimica et cosmochimica acta - New York, NY [u.a.] : Elsevier, 1950, 316, Seite 122-134
Übergeordnetes Werk:	volume:316 ; pages:122-134

DOI / URN:	10.1016/j.gca.2021.10.019

Katalog-ID:	ELV00694812X

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520			\|a Antimony (Sb) is a re-emerging contaminant, and its redox transformation is mainly driven by microorganisms. Sb(III) oxidation has been attributed to enzymatic catalyzed reaction, though the physiological reason for this process remains unclear. Herein, we isolated a bacterium named Pseudomonas sp. SbB1 which can oxidize Sb(III) to Sb(V) without known Sb-oxidizing genes in its genome. The Sb(III) oxidation followed a zero-order kinetics with an appreciably lower rate (0.068 μM/h) than known Sb(III) oxidases (0.159–0.210 μM/h). Our incubation experiments show that Sb(III) was oxidized by extracellular superoxide and the superoxide production is NADH-dependent. By in-gel analysis and Sb K-edge XANES, we found proteins at ∼100 kDa position were responsible for Sb(III) oxidation by producing superoxide. Further, our nano LC-MS/MS results suggest that dihydrolipoyl dehydrogenase was the source of extracellular superoxide. In vivo evidence with mutant indicated that strain ΔdldH was incapable of producing superoxide and oxidizing Sb(III), whereas complementation by dldH rescued the mutant’s ability. Beyond strain SbB1, superoxide generation and Sb(III) oxidation were also observed in diverse bacteria with DLDH orthologous across five classes. Our finding shows a previously unknown pathway used by widespread bacteria to mediate the transformation of redox-sensitive pollutants in the environment.
650		4	\|a Antimonite oxidation
650		4	\|a Microbial extracellular superoxide
650		4	\|a Redox transformation
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700	1		\|a Yin, Zhipeng \|e verfasserin \|4 aut
700	1		\|a Zhang, Lixin \|e verfasserin \|4 aut
700	1		\|a Jing, Chuanyong \|e verfasserin \|4 aut
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author_variant	l w lw l y ly z y zy l z lz c j cj
matchkey_str	article:00167037:2021----::nioiexdtobmcoilxrcl
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publishDate	2021
allfields	10.1016/j.gca.2021.10.019 doi (DE-627)ELV00694812X (ELSEVIER)S0016-7037(21)00622-0 DE-627 ger DE-627 rda eng 550 DE-600 38.32 bkl 39.29 bkl Wang, Liying verfasserin aut Antimonite oxidation by microbial extracellular superoxide in 2021 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Antimony (Sb) is a re-emerging contaminant, and its redox transformation is mainly driven by microorganisms. Sb(III) oxidation has been attributed to enzymatic catalyzed reaction, though the physiological reason for this process remains unclear. Herein, we isolated a bacterium named Pseudomonas sp. SbB1 which can oxidize Sb(III) to Sb(V) without known Sb-oxidizing genes in its genome. The Sb(III) oxidation followed a zero-order kinetics with an appreciably lower rate (0.068 μM/h) than known Sb(III) oxidases (0.159–0.210 μM/h). Our incubation experiments show that Sb(III) was oxidized by extracellular superoxide and the superoxide production is NADH-dependent. By in-gel analysis and Sb K-edge XANES, we found proteins at ∼100 kDa position were responsible for Sb(III) oxidation by producing superoxide. Further, our nano LC-MS/MS results suggest that dihydrolipoyl dehydrogenase was the source of extracellular superoxide. In vivo evidence with mutant indicated that strain ΔdldH was incapable of producing superoxide and oxidizing Sb(III), whereas complementation by dldH rescued the mutant’s ability. Beyond strain SbB1, superoxide generation and Sb(III) oxidation were also observed in diverse bacteria with DLDH orthologous across five classes. Our finding shows a previously unknown pathway used by widespread bacteria to mediate the transformation of redox-sensitive pollutants in the environment. Antimonite oxidation Microbial extracellular superoxide Redox transformation Ye, Li verfasserin aut Yin, Zhipeng verfasserin aut Zhang, Lixin verfasserin aut Jing, Chuanyong verfasserin aut Enthalten in Geochimica et cosmochimica acta New York, NY [u.a.] : Elsevier, 1950 316, Seite 122-134 Online-Ressource (DE-627)300898797 (DE-600)1483679-8 (DE-576)120883465 0016-7037 nnns volume:316 pages:122-134 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OPC-GGO SSG-OPC-AST GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 38.32 Geochemie 39.29 Theoretische Astronomie: Sonstiges AR 316 122-134
spelling	10.1016/j.gca.2021.10.019 doi (DE-627)ELV00694812X (ELSEVIER)S0016-7037(21)00622-0 DE-627 ger DE-627 rda eng 550 DE-600 38.32 bkl 39.29 bkl Wang, Liying verfasserin aut Antimonite oxidation by microbial extracellular superoxide in 2021 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Antimony (Sb) is a re-emerging contaminant, and its redox transformation is mainly driven by microorganisms. Sb(III) oxidation has been attributed to enzymatic catalyzed reaction, though the physiological reason for this process remains unclear. Herein, we isolated a bacterium named Pseudomonas sp. SbB1 which can oxidize Sb(III) to Sb(V) without known Sb-oxidizing genes in its genome. The Sb(III) oxidation followed a zero-order kinetics with an appreciably lower rate (0.068 μM/h) than known Sb(III) oxidases (0.159–0.210 μM/h). Our incubation experiments show that Sb(III) was oxidized by extracellular superoxide and the superoxide production is NADH-dependent. By in-gel analysis and Sb K-edge XANES, we found proteins at ∼100 kDa position were responsible for Sb(III) oxidation by producing superoxide. Further, our nano LC-MS/MS results suggest that dihydrolipoyl dehydrogenase was the source of extracellular superoxide. In vivo evidence with mutant indicated that strain ΔdldH was incapable of producing superoxide and oxidizing Sb(III), whereas complementation by dldH rescued the mutant’s ability. Beyond strain SbB1, superoxide generation and Sb(III) oxidation were also observed in diverse bacteria with DLDH orthologous across five classes. Our finding shows a previously unknown pathway used by widespread bacteria to mediate the transformation of redox-sensitive pollutants in the environment. Antimonite oxidation Microbial extracellular superoxide Redox transformation Ye, Li verfasserin aut Yin, Zhipeng verfasserin aut Zhang, Lixin verfasserin aut Jing, Chuanyong verfasserin aut Enthalten in Geochimica et cosmochimica acta New York, NY [u.a.] : Elsevier, 1950 316, Seite 122-134 Online-Ressource (DE-627)300898797 (DE-600)1483679-8 (DE-576)120883465 0016-7037 nnns volume:316 pages:122-134 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OPC-GGO SSG-OPC-AST GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 38.32 Geochemie 39.29 Theoretische Astronomie: Sonstiges AR 316 122-134
allfields_unstemmed	10.1016/j.gca.2021.10.019 doi (DE-627)ELV00694812X (ELSEVIER)S0016-7037(21)00622-0 DE-627 ger DE-627 rda eng 550 DE-600 38.32 bkl 39.29 bkl Wang, Liying verfasserin aut Antimonite oxidation by microbial extracellular superoxide in 2021 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Antimony (Sb) is a re-emerging contaminant, and its redox transformation is mainly driven by microorganisms. Sb(III) oxidation has been attributed to enzymatic catalyzed reaction, though the physiological reason for this process remains unclear. Herein, we isolated a bacterium named Pseudomonas sp. SbB1 which can oxidize Sb(III) to Sb(V) without known Sb-oxidizing genes in its genome. The Sb(III) oxidation followed a zero-order kinetics with an appreciably lower rate (0.068 μM/h) than known Sb(III) oxidases (0.159–0.210 μM/h). Our incubation experiments show that Sb(III) was oxidized by extracellular superoxide and the superoxide production is NADH-dependent. By in-gel analysis and Sb K-edge XANES, we found proteins at ∼100 kDa position were responsible for Sb(III) oxidation by producing superoxide. Further, our nano LC-MS/MS results suggest that dihydrolipoyl dehydrogenase was the source of extracellular superoxide. In vivo evidence with mutant indicated that strain ΔdldH was incapable of producing superoxide and oxidizing Sb(III), whereas complementation by dldH rescued the mutant’s ability. Beyond strain SbB1, superoxide generation and Sb(III) oxidation were also observed in diverse bacteria with DLDH orthologous across five classes. Our finding shows a previously unknown pathway used by widespread bacteria to mediate the transformation of redox-sensitive pollutants in the environment. Antimonite oxidation Microbial extracellular superoxide Redox transformation Ye, Li verfasserin aut Yin, Zhipeng verfasserin aut Zhang, Lixin verfasserin aut Jing, Chuanyong verfasserin aut Enthalten in Geochimica et cosmochimica acta New York, NY [u.a.] : Elsevier, 1950 316, Seite 122-134 Online-Ressource (DE-627)300898797 (DE-600)1483679-8 (DE-576)120883465 0016-7037 nnns volume:316 pages:122-134 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OPC-GGO SSG-OPC-AST GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 38.32 Geochemie 39.29 Theoretische Astronomie: Sonstiges AR 316 122-134
allfieldsGer	10.1016/j.gca.2021.10.019 doi (DE-627)ELV00694812X (ELSEVIER)S0016-7037(21)00622-0 DE-627 ger DE-627 rda eng 550 DE-600 38.32 bkl 39.29 bkl Wang, Liying verfasserin aut Antimonite oxidation by microbial extracellular superoxide in 2021 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Antimony (Sb) is a re-emerging contaminant, and its redox transformation is mainly driven by microorganisms. Sb(III) oxidation has been attributed to enzymatic catalyzed reaction, though the physiological reason for this process remains unclear. Herein, we isolated a bacterium named Pseudomonas sp. SbB1 which can oxidize Sb(III) to Sb(V) without known Sb-oxidizing genes in its genome. The Sb(III) oxidation followed a zero-order kinetics with an appreciably lower rate (0.068 μM/h) than known Sb(III) oxidases (0.159–0.210 μM/h). Our incubation experiments show that Sb(III) was oxidized by extracellular superoxide and the superoxide production is NADH-dependent. By in-gel analysis and Sb K-edge XANES, we found proteins at ∼100 kDa position were responsible for Sb(III) oxidation by producing superoxide. Further, our nano LC-MS/MS results suggest that dihydrolipoyl dehydrogenase was the source of extracellular superoxide. In vivo evidence with mutant indicated that strain ΔdldH was incapable of producing superoxide and oxidizing Sb(III), whereas complementation by dldH rescued the mutant’s ability. Beyond strain SbB1, superoxide generation and Sb(III) oxidation were also observed in diverse bacteria with DLDH orthologous across five classes. Our finding shows a previously unknown pathway used by widespread bacteria to mediate the transformation of redox-sensitive pollutants in the environment. Antimonite oxidation Microbial extracellular superoxide Redox transformation Ye, Li verfasserin aut Yin, Zhipeng verfasserin aut Zhang, Lixin verfasserin aut Jing, Chuanyong verfasserin aut Enthalten in Geochimica et cosmochimica acta New York, NY [u.a.] : Elsevier, 1950 316, Seite 122-134 Online-Ressource (DE-627)300898797 (DE-600)1483679-8 (DE-576)120883465 0016-7037 nnns volume:316 pages:122-134 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OPC-GGO SSG-OPC-AST GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 38.32 Geochemie 39.29 Theoretische Astronomie: Sonstiges AR 316 122-134
allfieldsSound	10.1016/j.gca.2021.10.019 doi (DE-627)ELV00694812X (ELSEVIER)S0016-7037(21)00622-0 DE-627 ger DE-627 rda eng 550 DE-600 38.32 bkl 39.29 bkl Wang, Liying verfasserin aut Antimonite oxidation by microbial extracellular superoxide in 2021 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Antimony (Sb) is a re-emerging contaminant, and its redox transformation is mainly driven by microorganisms. Sb(III) oxidation has been attributed to enzymatic catalyzed reaction, though the physiological reason for this process remains unclear. Herein, we isolated a bacterium named Pseudomonas sp. SbB1 which can oxidize Sb(III) to Sb(V) without known Sb-oxidizing genes in its genome. The Sb(III) oxidation followed a zero-order kinetics with an appreciably lower rate (0.068 μM/h) than known Sb(III) oxidases (0.159–0.210 μM/h). Our incubation experiments show that Sb(III) was oxidized by extracellular superoxide and the superoxide production is NADH-dependent. By in-gel analysis and Sb K-edge XANES, we found proteins at ∼100 kDa position were responsible for Sb(III) oxidation by producing superoxide. Further, our nano LC-MS/MS results suggest that dihydrolipoyl dehydrogenase was the source of extracellular superoxide. In vivo evidence with mutant indicated that strain ΔdldH was incapable of producing superoxide and oxidizing Sb(III), whereas complementation by dldH rescued the mutant’s ability. Beyond strain SbB1, superoxide generation and Sb(III) oxidation were also observed in diverse bacteria with DLDH orthologous across five classes. Our finding shows a previously unknown pathway used by widespread bacteria to mediate the transformation of redox-sensitive pollutants in the environment. Antimonite oxidation Microbial extracellular superoxide Redox transformation Ye, Li verfasserin aut Yin, Zhipeng verfasserin aut Zhang, Lixin verfasserin aut Jing, Chuanyong verfasserin aut Enthalten in Geochimica et cosmochimica acta New York, NY [u.a.] : Elsevier, 1950 316, Seite 122-134 Online-Ressource (DE-627)300898797 (DE-600)1483679-8 (DE-576)120883465 0016-7037 nnns volume:316 pages:122-134 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OPC-GGO SSG-OPC-AST GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 38.32 Geochemie 39.29 Theoretische Astronomie: Sonstiges AR 316 122-134
language	English
source	Enthalten in Geochimica et cosmochimica acta 316, Seite 122-134 volume:316 pages:122-134
sourceStr	Enthalten in Geochimica et cosmochimica acta 316, Seite 122-134 volume:316 pages:122-134
format_phy_str_mv	Article
bklname	Geochemie Theoretische Astronomie: Sonstiges
institution	findex.gbv.de
topic_facet	Antimonite oxidation Microbial extracellular superoxide Redox transformation
dewey-raw	550
isfreeaccess_bool	false
container_title	Geochimica et cosmochimica acta
authorswithroles_txt_mv	Wang, Liying @@aut@@ Ye, Li @@aut@@ Yin, Zhipeng @@aut@@ Zhang, Lixin @@aut@@ Jing, Chuanyong @@aut@@
publishDateDaySort_date	2021-01-01T00:00:00Z
hierarchy_top_id	300898797
dewey-sort	3550
id	ELV00694812X
language_de	englisch
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author	Wang, Liying
spellingShingle	Wang, Liying ddc 550 bkl 38.32 bkl 39.29 misc Antimonite oxidation misc Microbial extracellular superoxide misc Redox transformation Antimonite oxidation by microbial extracellular superoxide in
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topic_title	550 DE-600 38.32 bkl 39.29 bkl Antimonite oxidation by microbial extracellular superoxide in Antimonite oxidation Microbial extracellular superoxide Redox transformation
topic	ddc 550 bkl 38.32 bkl 39.29 misc Antimonite oxidation misc Microbial extracellular superoxide misc Redox transformation
topic_unstemmed	ddc 550 bkl 38.32 bkl 39.29 misc Antimonite oxidation misc Microbial extracellular superoxide misc Redox transformation
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title	Antimonite oxidation by microbial extracellular superoxide in
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title_full	Antimonite oxidation by microbial extracellular superoxide in
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title_sort	antimonite oxidation by microbial extracellular superoxide in
title_auth	Antimonite oxidation by microbial extracellular superoxide in
abstract	Antimony (Sb) is a re-emerging contaminant, and its redox transformation is mainly driven by microorganisms. Sb(III) oxidation has been attributed to enzymatic catalyzed reaction, though the physiological reason for this process remains unclear. Herein, we isolated a bacterium named Pseudomonas sp. SbB1 which can oxidize Sb(III) to Sb(V) without known Sb-oxidizing genes in its genome. The Sb(III) oxidation followed a zero-order kinetics with an appreciably lower rate (0.068 μM/h) than known Sb(III) oxidases (0.159–0.210 μM/h). Our incubation experiments show that Sb(III) was oxidized by extracellular superoxide and the superoxide production is NADH-dependent. By in-gel analysis and Sb K-edge XANES, we found proteins at ∼100 kDa position were responsible for Sb(III) oxidation by producing superoxide. Further, our nano LC-MS/MS results suggest that dihydrolipoyl dehydrogenase was the source of extracellular superoxide. In vivo evidence with mutant indicated that strain ΔdldH was incapable of producing superoxide and oxidizing Sb(III), whereas complementation by dldH rescued the mutant’s ability. Beyond strain SbB1, superoxide generation and Sb(III) oxidation were also observed in diverse bacteria with DLDH orthologous across five classes. Our finding shows a previously unknown pathway used by widespread bacteria to mediate the transformation of redox-sensitive pollutants in the environment.
abstractGer	Antimony (Sb) is a re-emerging contaminant, and its redox transformation is mainly driven by microorganisms. Sb(III) oxidation has been attributed to enzymatic catalyzed reaction, though the physiological reason for this process remains unclear. Herein, we isolated a bacterium named Pseudomonas sp. SbB1 which can oxidize Sb(III) to Sb(V) without known Sb-oxidizing genes in its genome. The Sb(III) oxidation followed a zero-order kinetics with an appreciably lower rate (0.068 μM/h) than known Sb(III) oxidases (0.159–0.210 μM/h). Our incubation experiments show that Sb(III) was oxidized by extracellular superoxide and the superoxide production is NADH-dependent. By in-gel analysis and Sb K-edge XANES, we found proteins at ∼100 kDa position were responsible for Sb(III) oxidation by producing superoxide. Further, our nano LC-MS/MS results suggest that dihydrolipoyl dehydrogenase was the source of extracellular superoxide. In vivo evidence with mutant indicated that strain ΔdldH was incapable of producing superoxide and oxidizing Sb(III), whereas complementation by dldH rescued the mutant’s ability. Beyond strain SbB1, superoxide generation and Sb(III) oxidation were also observed in diverse bacteria with DLDH orthologous across five classes. Our finding shows a previously unknown pathway used by widespread bacteria to mediate the transformation of redox-sensitive pollutants in the environment.
abstract_unstemmed	Antimony (Sb) is a re-emerging contaminant, and its redox transformation is mainly driven by microorganisms. Sb(III) oxidation has been attributed to enzymatic catalyzed reaction, though the physiological reason for this process remains unclear. Herein, we isolated a bacterium named Pseudomonas sp. SbB1 which can oxidize Sb(III) to Sb(V) without known Sb-oxidizing genes in its genome. The Sb(III) oxidation followed a zero-order kinetics with an appreciably lower rate (0.068 μM/h) than known Sb(III) oxidases (0.159–0.210 μM/h). Our incubation experiments show that Sb(III) was oxidized by extracellular superoxide and the superoxide production is NADH-dependent. By in-gel analysis and Sb K-edge XANES, we found proteins at ∼100 kDa position were responsible for Sb(III) oxidation by producing superoxide. Further, our nano LC-MS/MS results suggest that dihydrolipoyl dehydrogenase was the source of extracellular superoxide. In vivo evidence with mutant indicated that strain ΔdldH was incapable of producing superoxide and oxidizing Sb(III), whereas complementation by dldH rescued the mutant’s ability. Beyond strain SbB1, superoxide generation and Sb(III) oxidation were also observed in diverse bacteria with DLDH orthologous across five classes. Our finding shows a previously unknown pathway used by widespread bacteria to mediate the transformation of redox-sensitive pollutants in the environment.
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title_short	Antimonite oxidation by microbial extracellular superoxide in
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up_date	2024-07-06T23:05:57.421Z
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