ArticleThe Journal of biological chemistry2011
Structural basis for the oxidation of protein-bound sulfur by the sulfur cycle molybdohemo-enzyme sulfane dehydrogenase SoxCD.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 56 citations in OpenAlex.
- A Dinuclear Iron(II) Persulfide Complex Reacts with OJournal of the American Chemical Society · 2026Article
- An ArsR-type transcriptional regulator, SoxR, regulates sulfur oxidization (Sox) system in Cupriavidus pinatubonensis JMP134.BMC microbiology · 2026Article
- Carbon, nitrogen, and sulfur cycling unveil deep-sea microbial niches in the Atacama Trench.Nature communications · 2026Article
- pH and thiosulfate dependent microbial sulfur oxidation strategies across diverse environments.Frontiers in microbiology · 2024Article
- In the AlphaproteobacteriumAntioxidants (Basel, Switzerland) · 2023Article
- The evolution and spread of sulfur cycling enzymes reflect the redox state of the early Earth.Science advances · 2023Article
- A CsoR family transcriptional regulator, TTHA1953, controls the sulfur oxidation pathway in Thermus thermophilus HB8.The Journal of biological chemistry · 2023Article
- Cold Sulfur Springs-Neglected Niche for Autotrophic Sulfur-Oxidizing Bacteria.Microorganisms · 2023Review
- Article
- Biodesulfurization Induces Reprogramming of Sulfur Metabolism in Rhodococcus qingshengii IGTS8: Proteomics and Untargeted Metabolomics.Microbiology spectrum · 2021Article
- Marinobacter orientalis sp. nov., a thiosulfate-oxidizing bacterium isolated from a marine solar saltern.Antonie van Leeuwenhoek · 2021Article
- The Heterotrophic Bacterium Cupriavidus pinatubonensis JMP134 Oxidizes Sulfide to Sulfate with Thiosulfate as a Key Intermediate.Applied and environmental microbiology · 2020Article
- Genomes of Neutrophilic Sulfur-Oxidizing Chemolithoautotrophs Representing 9 Proteobacterial Species From 8 Genera.Frontiers in microbiology · 2019Article
- Sulfur Oxidation in the Acidophilic AutotrophicFrontiers in microbiology · 2018Review
- Genome features of moderately halophilic polyhydroxyalkanoate-producingStandards in genomic sciences · 2017Article
- Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ.PloS one · 2017Article
- Thiosulfate oxidation by Thiomicrospira thermophila: metabolic flexibility in response to ambient geochemistry.Environmental microbiology · 2016Article
- Complete genome sequence of the haloalkaliphilic, obligately chemolithoautotrophic thiosulfate and sulfide-oxidizing γ-proteobacterium Thioalkalimicrobium cyclicum type strain ALM 1 (DSM 14477(T)).Standards in genomic sciences · 2016Article
- Structural Stability, Transitions, and Interactions within SoxYZCD-Thiosulphate fromJournal of biophysics (Hindawi Publishing Corporation : Online) · 2016Article
- Structural basis for specificity and promiscuity in a carrier protein/enzyme system from the sulfur cycle.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sulfur cycle enzyme sulfane dehydrogenase SoxCD is an essential component of the sulfur oxidation (Sox) enzyme system of Paracoccus pantotrophus. SoxCD catalyzes a six-electron oxidation reaction within the Sox cycle. SoxCD is an α(2)β(2) heterotetrameric complex of the molybdenum cofactor-containing SoxC protein and the diheme c-type cytochrome SoxD with the heme domains D(1) and D(2). SoxCD(1) misses the heme-2 domain D(2) and is catalytically as active as SoxCD. The crystal structure of SoxCD(1) was solved at 1.33 Å. The substrate of SoxCD is the outer (sulfane) sulfur of Cys-110-persulfide located at the C-terminal peptide swinging arm of SoxY of the SoxYZ carrier complex. The SoxCD(1) substrate funnel toward the molybdopterin is narrow and partially shielded by side-chain residues of SoxD(1). For access of the sulfane-sulfur of SoxY-Cys-110 persulfide we propose that (i) the blockage by SoxD-Arg-98 is opened via interaction with the C terminus of SoxY and (ii) the C-terminal peptide VTIGGCGG of SoxY provides interactions with the entrance path such that the cysteine-bound persulfide is optimally positioned near the molybdenum atom. The subsequent oxidation reactions of the sulfane-sulfur are initiated by the nucleophilic attack of the persulfide anion on the molybdenum atom that is, in turn, reduced. The close proximity of heme-1 to the molybdopterin allows easy acceptance of the electrons. Because SoxYZ, SoxXA, and SoxB are already structurally characterized, with SoxCD(1) the structures of all key enzymes of the Sox cycle are known with atomic resolution.
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