Immunocytochemical localization of APS reductase and bisulfite reductase in three Desulfovibrio species

Abstract

IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document VersionPublisher's PDF, also known as Version of record Publication date: 1988 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Kremer, D. R., Veenhuis, M., Fauque, G., Peck Jr., H. D., LeGall, J., Lampreia, J., ... Hansen, T. A. (1988). Immunocytochemical localization of APS reductase and bisulfite reductase in three Desulfovibrio species. Archives of Microbiology, 150(3). https://doi.org/10.1007/BF00407795 Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons).Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. with APS reductase antibodies resulted in a distribution of gold particles over the cytoplasmic membrane region. The localization of the two enzymes is discussed with respect to the mechanism and energetics of dissimilatory sulfate reduction. Key words:Desulfovibrio -Dissimilatory sulfate reduction -APS reductase -Bisulfite reductase -Enzyme localization -Immunogold labeling Dissimilatory sulfate reduction is carried out by a large variety of bacteria (Hansen 1988;Widdel 1988). Most studies on its mechanism have been confined to bacteria belonging to the genus Desulfovibrio (Peck and LeGall 1982;LeGall and Fauque 1988). Dissimilatory sulfate reduction proceeds as follows:Sulfate is activated by ATP-sulfurylase to adenosine phosphosulfate (APS), which is subsequently reduced to sulfite plus AMP by the enzyme APS reductase (LeGall and Fauque 1988). In D. vulgaris Hildenborough APS reductase is a non-heme iron flavoprotein containing two different subunits, of 72 kD and 20 kD molecular mass, but it has an unknown subunit structure (Bramlett and Peck 1975). Its natural electron donor is not known. APS reductase has been detected in several genera of sulfate-reducing bacteria (Stille and Triiper 1984). Offprint requests to: T. A. HansenThe biochemistry of the reduction of sulfite to sulfide is somewhat controversial. A cyclic route, the so-called trithionate pathway, has been postulated, in which trithionate and thiosulfate are intermediates (Akagi 1981). In this route sulfite is first reduced to trithionate by the enzyme bisulfite reductase. However, strong indications were found that in Desulfovibrio spp. this is not the natural pathway (Chambers and Trudinger 1975;LeGall and Fauque 1988) and that in vivo a direct six electron reduction of sulfite to sulfide by the enzyme bisulfite reductase may occur. Whatever route is functioning, bisulfite reductase plays a key role in the dissimilatory reduction of sulfite. Four classes of bisulfite reductas...

The active centers of adenylylsulfate reductase from Desulfovibrio gigas

“…However, it was recently found that in Desuljbvibrio thermophilus, AdoPSO, reductase is clearly membrane associated [5], as in the case of the enzyme isolated from purple sulfur bacteria belonging to the Chromutiaceue species, where AdoPS04 reductase is associated with the chromatophores [6]. Tetrahemic cytochrome c3 (13 kDa), ferredoxin and flavodoxin stimulate the reduction of sulfate but werc not demonstrated conclusively to be donors ofelectrons to the reductase [7].…”

Purification and biochemical characterization of a putative [6Fe‐6S] prismane‐cluster‐containing protein from Desulfovibrio vulgaris (Hildenborough)

“…From the EDTA extractability [22] and membrane-translocation mechanism [Sl] it is known that in D . vulgaris (Hildenborough) a highly active Fe-hydrogenase resides in the periplasm, whereas APS reductase and dissimilatory sulfite reductase (desulfoviridin) are present in the cytoplasm [52]. These enzymes were used as convenient markers in our fractionation procedure.…”

“…Although it is possible that Fig. 4 the protein was released from membranes during the process of cell disruption [52], the absence of a relevant immunoblot response of the membrane fraction strongly argues against this possibility. A fully soluble nature of the prismane protein is also indicated by both amino acid composition (Table 4) and aqueous solubility ( > 40 mg/ml).…”

Crystal Structure of Adenylylsulfate Reductase fromDesulfovibrio gigasSuggests a Potential Self-Regulation Mechanism Involving the C Terminus of the β-Subunit

“…APSR was first partially purified and characterized from Desulfovibrio desulfuricans (32). Multiple forms of APSR in Desulfovibrio vulgaris were ob-served in buffers under varied conditions (1) and were found in the cytoplasm of cells (18). APSR from D. gigas was first purified by Lampreia et al (21) and showed a molecular mass of 400 kDa comprised of ␣-and ␤-subunits, corresponding to the molecular masses of 70 kDa and 23 kDa, respectively.…”