Acts as an electron acceptor for the thiosulfate dehydrogenase TsdA.
MRQFIPMRRVLAVATLGALFWAAPASWAAAPPEAASCIACHGAGGMGNPAAGYPRLAGLP
EQYLADQLRYFADGARNNAVMSGMAKPLSAAQVTALATYYSKLKPSGKPAPMPTGAAAAE
GERLALRGDWEKGIPACIRCHGPGAVGVGENFPALVGQSAAYIEAQIKAWKDGSRSGDPL
GLMHTVALRMTDAQTQAVAQWLAAQPLSPTKSASAKH220
| PMID | Title & Author | Abstract | Year | |
| 0 | 27694441 | Electron Accepting Units of the Diheme Cytochrome c TsdA, a Bifunctional Thiosulfate Dehydrogenase/Tetrathionate Reductase. Kurth JM, Brito JA, Reuter J, Flegler A, Koch T, Franke T, Klein EM, Rowe SF, Butt JN, Denkmann K, Pereira IA, Archer M, Dahl C. | The enzymes of the thiosulfate dehydrogenase (TsdA) family are wide-spread diheme c-type cytochromes. Here, redox carriers were studied mediating the flow of electrons arising from thiosulfate oxidation into respiratory or photosynthetic electron chains. In a number of organisms, including Thiomonas intermedia and Sideroxydans lithotrophicus, the tsdA gene is immediately preceded by tsdB encoding for another diheme cytochrome. Spectrophotometric experiments in combination with enzymatic assays in solution showed that TsdB acts as an effective electron acceptor of TsdA in vitro when TsdA and TsdB originate from the same source organism. Although TsdA covers a range from -300 to +150 mV, TsdB is redox active between -100 and +300 mV, thus enabling electron transfer between these hemoproteins. The three-dimensional structure of the TsdB-TsdA fusion protein from the purple sulfur bacterium Marichromatium purpuratum was solved by X-ray crystallography to 2.75 Å resolution providing insights into internal electron transfer. In the oxidized state, this tetraheme cytochrome c contains three hemes with axial His/Met ligation, whereas heme 3 exhibits the His/Cys coordination typical for TsdA active sites. Interestingly, thiosulfate is covalently bound to Cys330 on heme 3. In several bacteria, including Allochromatium vinosum, TsdB is not present, precluding a general and essential role for electron flow. Both AvTsdA and the MpTsdBA fusion react efficiently in vitro with high potential iron-sulfur protein from A. vinosum (Em +350 mV). High potential iron-sulfur protein not only acts as direct electron donor to the reaction center in anoxygenic phototrophs but can also be involved in aerobic respiratory chains. | 2016 |
| 1 | 26319878 | γ-Resorcylate catabolic-pathway genes in the soil actinomycete Rhodococcus jostii RHA1. Kasai D, Araki N, Motoi K, Yoshikawa S, Iino T, Imai S, Masai E, Fukuda M. | The Rhodococcus jostii RHA1 gene cluster required for γ-resorcylate (GRA) catabolism was characterized. The cluster includes tsdA, tsdB, tsdC, tsdD, tsdR, tsdT, and tsdX, which encode GRA decarboxylase, resorcinol 4-hydroxylase, hydroxyquinol 1,2-dioxygenase, maleylacetate reductase, an IclR-type regulator, a major facilitator superfamily transporter, and a putative hydrolase, respectively. The tsdA gene conferred GRA decarboxylase activity on Escherichia coli. Purified TsdB oxidized NADH in the presence of resorcinol, suggesting that tsdB encodes a unique NADH-specific single-component resorcinol 4-hydroxylase. Mutations in either tsdA or tsdB resulted in growth deficiency on GRA. The tsdC and tsdD genes conferred hydroxyquinol 1,2-dioxygenase and maleylacetate reductase activities, respectively, on E. coli. Inactivation of tsdT significantly retarded the growth of RHA1 on GRA. The growth retardation was partially suppressed under acidic conditions, suggesting the involvement of tsdT in GRA uptake. Reverse transcription-PCR analysis revealed that the tsd genes constitute three transcriptional units, the tsdBADC and tsdTX operons and tsdR. Transcription of the tsdBADC and tsdTX operons was induced during growth on GRA. Inactivation of tsdR derepressed transcription of the tsdBADC and tsdTX operons in the absence of GRA, suggesting that tsd gene transcription is negatively regulated by the tsdR-encoded regulator. Binding of TsdR to the tsdR-tsdB and tsdT-tsdR intergenic regions was inhibited by the addition of GRA, indicating that GRA interacts with TsdR as an effector molecule. | 2015 |
| 2 | 28380974 | Waveguiding characteristics of surface enhanced Raman scattering signals along crystalline organic semiconducting microrod. Jo SG, Kim BG, Kim J, Kim J, Joo J. | The waveguiding of surface enhanced Raman scattering (SERS) signals was demonstrated by using organic semiconducting microrods (MRs) hybridized with functionalized gold nanoparticles (Au-NPs). Organic semiconducting 1,4-bis(3,5-bis(trifluoromethyl) styryl)-2,5-dibromobenzene (TSDB) crystalline MRs were fabricated as active optical waveguiding system using a self-assembly method. The static SERS effect and the enhancement of photoluminescence were simultaneously observed for the TSDB MRs hybridized with Au-NPs. The waveguiding characteristics of the SERS signals through the hybrid MR of TSDB/Au-NPs were investigated using a high-resolution laser confocal microscope (LCM) system. The enhanced output Raman characteristic modes of TSDB molecules were clearly observed along the hybrid MR of TSDB/Au-NPs, which is attributed to stronger scattering of the light and the increased coupling efficiency of waveguiding due to the presence of Au-NPs. The waveguiding of the SERS signals exhibited different decay constants for the corresponding characteristic Raman modes, such as -C = C- aromatic, -CF3, and C-Br stretching modes. The observed waveguiding characteristics of various SERS modes enable multi-modal waveguiding with relatively narrow spectral resolution for nanophotonic information. | 2017 |
Kurth J M, Brito J A, Reuter J, et al. Electron accepting units of the diheme cytochrome c TsdA, a bifunctional thiosulfate dehydrogenase/tetrathionate reductase[J]. Journal of Biological Chemistry, 2016, 291(48): 24804-24818.