A cascade of sulfur transferases delivers sulfur to the sulfur-oxidizing heterodisulfide reductase-like complex DOI Creative Commons
Tomohisa Sebastian Tanabe,

Elena Bach,

Giulia D’Ermo

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2023, Volume and Issue: unknown

Published: Dec. 18, 2023

ABSTRACT A heterodisulfide reductase-like complex (sHdr) and novel lipoate-binding proteins (LbpAs) are central players of a wide-spread pathway dissimilatory sulfur oxidation. Bioinformatic analysis demonstrate that the cytoplasmic sHdr-LbpA systems always accompanied by sets transferases (DsrE proteins, TusA, rhodaneses). The exact composition these may vary depending on organism sHdr system type. To enable generalizations, we studied model oxidizers from distant bacterial phyla, i.e. Aquificota Pseudomonadota. DsrE3C chemoorganotrophic Alphaproteobacterium Hyphomicrobium denitrificans DsrE3B Gammaproteobacteria Thioalkalivibrio sp. K90mix, an obligate chemolithotroph, Thiorhodospira sibirica , photolithotroph, homotrimers donate to TusA. Additionally, hyphomicrobial rhodanese-like protein Rhd442 exchanges with both TusA DsrE3C. latter is essential for oxidation in Hm. . Aquifex aeolicus (AqTusA) interacts physiologically AqDsrE, AqLbpA AqsHdr proteins. This particularly significant as it establishes direct link between oxidizes sulfane sulfite. In vivo, unlikely there strict unidirectional transfer sulfur-binding enzymes studied. Rather, form network, each pool bound sulfur. Sulfur flux can then be shifted one direction or other metabolic requirements. single pair preferred direction, such DsrE3-type towards sufficient push into sink where further metabolized needed. SIGNIFICANCE STATEMENT network uncovered characterized ultimately delivers sulfur-oxidizing metalloenzyme, sHdr, resembles reductase methanogenic archaea Similar occur phylogenetically bacteria, underscoring fundamental importance work.

Language: Английский

A cascade of sulfur transferases delivers sulfur to the sulfur‐oxidizing heterodisulfide reductase‐like complex DOI Creative Commons
Tomohisa Sebastian Tanabe,

Elena Bach,

Giulia D’Ermo

et al.

Protein Science, Journal Year: 2024, Volume and Issue: 33(6)

Published: May 15, 2024

A heterodisulfide reductase-like complex (sHdr) and novel lipoate-binding proteins (LbpAs) are central players of a wide-spread pathway dissimilatory sulfur oxidation. Bioinformatic analysis demonstrate that the cytoplasmic sHdr-LbpA systems always accompanied by sets transferases (DsrE proteins, TusA, rhodaneses). The exact composition these may vary depending on organism sHdr system type. To enable generalizations, we studied model oxidizers from distant bacterial phyla, is, Aquificota Pseudomonadota. DsrE3C chemoorganotrophic Alphaproteobacterium Hyphomicrobium denitrificans DsrE3B Gammaproteobacteria Thioalkalivibrio sp. K90mix, an obligate chemolithotroph, Thiorhodospira sibirica, photolithotroph, homotrimers donate to TusA. Additionally, hyphomicrobial rhodanese-like protein Rhd442 exchanges with both TusA DsrE3C. latter is essential for oxidation in Hm. denitrificans. Aquifex aeolicus (AqTusA) interacts physiologically AqDsrE, AqLbpA, AqsHdr proteins. This particularly significant as it establishes direct link between oxidizes sulfane sulfite. In vivo, unlikely there strict unidirectional transfer sulfur-binding enzymes studied. Rather, form network, each pool bound sulfur. Sulfur flux can then be shifted one direction or other metabolic requirements. single pair preferred direction, such DsrE3-type towards sufficient push into sink where further metabolized needed.

Language: Английский

Citations

4
Microbiological Mechanisms and Effects of Dissimilatory Iron Reduction on Combined Contaminants Bio-Transformation: A Review DOI
Yue Yang, Haibo Li, Ye Yuan

et al.

Process Biochemistry, Journal Year: 2025, Volume and Issue: unknown

Published: March 1, 2025

Language: Английский

Citations

0
Deciphering microbial responses to H2S inhibition of typical functional microorganisms in anaerobic digestion ecosystems DOI Creative Commons

Wenhui Shu,

Bang Du,

Guangxue Wu

et al.

Chemical Engineering Journal, Journal Year: 2025, Volume and Issue: unknown, P. 162766 - 162766

Published: April 1, 2025

Language: Английский

Citations

0
Comprehensive evaluation of sulfur-siderite composite filler on load shock resistance of constructed wetlands under unsteady flow DOI
Rongzhen Wang,

Xuejun Zhang,

Jianchao Yang

et al.

Journal of environmental chemical engineering, Journal Year: 2025, Volume and Issue: unknown, P. 116787 - 116787

Published: April 1, 2025

Language: Английский

Citations

0
Mechanism of Intracellular Elemental Sulfur Oxidation in Beggiatoa leptomitoformis, Where Persulfide Dioxygenase Plays a Key Role DOI Open Access
Tatyana S. Rudenko, Liubov I. Trubitsina, Vasily V. Terentyev

et al.

International Journal of Molecular Sciences, Journal Year: 2024, Volume and Issue: 25(20), P. 10962 - 10962

Published: Oct. 11, 2024

Representatives of the colorless sulfur bacteria genus Beggiatoa use reduced compounds in processes lithotrophic growth, which is accompanied by storage intracellular sulfur. However, it still unknown how transformation occurs representatives. Annotation genome leptomitoformis D-402 did not identify any genes for oxidation or reduction elemental By searching BLASTP, two putative persulfide dioxygenase (PDO) homologs were found B. leptomitoformis. In some heterotrophic prokaryotes, PDO involved sulfane According to HPLC-MS/MS, revealed protein was reliably detected a culture sample grown only presence endogenous and CO2. The recombinant from active glutathione persulfide. crystal structure exhibited consistency with known structures type I PDO. Thus, shown that uses oxidize Additionally, on basis RT-qPCR, study reaction products, we predicted interrelation Sox-system function connection this process energy metabolism.

Language: Английский

Citations

1
YeeE-like bacterial SoxT proteins mediate sulfur import for oxidation and signal transduction DOI Creative Commons
Christiane Dahl, Jingjing Li,

Fabienne Göbel

et al.

Research Square (Research Square), Journal Year: 2024, Volume and Issue: unknown

Published: June 18, 2024

Abstract Many sulfur-oxidizing prokaryotes oxidize sulfur compounds through a combination of initial extracytoplasmic and downstream cytoplasmic reactions. Facultative oxidizers adjust transcription to availability. While enzymes transcriptional repressors have been extensively studied, import into the cytoplasm how regulators sense external are poorly understood. Addressing this gap, we show that SoxT1A SoxT1B, which resemble YeeE/YedE-family thiosulfate transporters encoded alongside oxidation regulation genes, fulfill these roles in Alphaproteobacterium Hyphomicrobium denitrificans. mutants oxidation-negative despite high levels showing delivers for its further oxidation. SoxT1B serves as signal transduction unit repressor SoxR, due low unless SoxR is also absent. Thus, play essential but distinct oxidative metabolism regulation.

Language: Английский

Citations

0
YeeE-like bacterial SoxT proteins mediate sulfur import for oxidation and signal transduction DOI Creative Commons
Jingjing Li,

Fabienne Göbel,

Hsun Yun Hsu

et al.

Communications Biology, Journal Year: 2024, Volume and Issue: 7(1)

Published: Nov. 21, 2024

Abstract Many sulfur-oxidizing prokaryotes oxidize sulfur compounds through a combination of initial extracytoplasmic and downstream cytoplasmic reactions. Facultative oxidizers adjust transcription to availability. While enzymes transcriptional repressors have been extensively studied, import into the cytoplasm how regulators sense external are poorly understood. Addressing this gap, we show that SoxT1A SoxT1B, which resemble YeeE/YedE-family thiosulfate transporters encoded alongside oxidation regulation genes, fulfill these roles in Alphaproteobacterium Hyphomicrobium denitrificans . mutants oxidation-negative despite high levels showing delivers for its further oxidation. SoxT1B serves as signal transduction unit repressor SoxR, due low unless SoxR is also absent. Thus, play essential but distinct oxidative metabolism regulation.

Language: Английский

Citations

0
A cascade of sulfur transferases delivers sulfur to the sulfur-oxidizing heterodisulfide reductase-like complex DOI Creative Commons
Tomohisa Sebastian Tanabe,

Elena Bach,

Giulia D’Ermo

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2023, Volume and Issue: unknown

Published: Dec. 18, 2023

ABSTRACT A heterodisulfide reductase-like complex (sHdr) and novel lipoate-binding proteins (LbpAs) are central players of a wide-spread pathway dissimilatory sulfur oxidation. Bioinformatic analysis demonstrate that the cytoplasmic sHdr-LbpA systems always accompanied by sets transferases (DsrE proteins, TusA, rhodaneses). The exact composition these may vary depending on organism sHdr system type. To enable generalizations, we studied model oxidizers from distant bacterial phyla, i.e. Aquificota Pseudomonadota. DsrE3C chemoorganotrophic Alphaproteobacterium Hyphomicrobium denitrificans DsrE3B Gammaproteobacteria Thioalkalivibrio sp. K90mix, an obligate chemolithotroph, Thiorhodospira sibirica , photolithotroph, homotrimers donate to TusA. Additionally, hyphomicrobial rhodanese-like protein Rhd442 exchanges with both TusA DsrE3C. latter is essential for oxidation in Hm. . Aquifex aeolicus (AqTusA) interacts physiologically AqDsrE, AqLbpA AqsHdr proteins. This particularly significant as it establishes direct link between oxidizes sulfane sulfite. In vivo, unlikely there strict unidirectional transfer sulfur-binding enzymes studied. Rather, form network, each pool bound sulfur. Sulfur flux can then be shifted one direction or other metabolic requirements. single pair preferred direction, such DsrE3-type towards sufficient push into sink where further metabolized needed. SIGNIFICANCE STATEMENT network uncovered characterized ultimately delivers sulfur-oxidizing metalloenzyme, sHdr, resembles reductase methanogenic archaea Similar occur phylogenetically bacteria, underscoring fundamental importance work.

Language: Английский

Citations

0