Heterodisulfide reductase (Hdr), is an iron-sulfur protein which in anaerobic methanogenic archaea catalyzes the reduction of the disulphide bond between coenzyme M and coenzyme B and is coupled to methane formation.
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| PMID | Title & Author | Abstract | Year | |
| 0 | Heterodisulfide Reductase from Acidithiobacilli is a Key Component Involved in Metabolism of Reduced Inorganic Sulfur Compounds. Ehrenfeld N , Levicán, Gloria, Parada P . | Heterodisulfide reductase (Hdr), is an iron-sulfur protein which in anaerobic methanogenic archaea catalyzes the reduction of the disulphide bond between coenzyme M and coenzyme B and is coupled to methane formation. In aerobic acidophilic chemolithotrophic bacteria (e.g., biomining bacteria) the function of this enzyme is unclear. Inspection of the genomic sequences of Acidithiobacillus ferrooxidans DSM 16786 and Acidithiobacillus thiooxidans DSM 17318 and reverse transcriptase-PCR results revealed a cluster of six co-transcribed genes, hdrC1, hdrB1, hdrA, orf1, hdrC2 and hdrB2, encoding proteins with high similarity to catalytic Hdr subunits. Additionally, microarray expression profiling and quantitative RT-PCR experiments demonstrated that the hdr genes of A. ferrooxidans and A. thiooxidans were highly expressed when bacteria are grown in the presence of sulfur and tetrathionate. Moreover, hdr genes in A. ferrooxidans were greatly up-regulated when this microorganism was grown in sulfur compared to ferrous medium. These results strongly support a role for Hdr in oxidative metabolism of reduced sulfur compounds in aerobic chemolithotrophic bacteria. | 2013 | |
| 1 | 27284018.0 | Microbial oxidative sulfur metabolism: biochemical evidence of the membrane-bound heterodisulfide reductase-like complex of the bacterium Aquifex aeolicus. Boughanemi S, Lyonnet J, Infossi P, Bauzan M, Kosta A, Lignon S, Giudici-Orticoni MT, Guiral M. | The Hdr (heterodisulfide reductase)-like enzyme is predicted, from gene transcript profiling experiments previously published, to be essential in oxidative sulfur metabolism in a number of bacteria and archaea. Nevertheless, no biochemical and physicochemical data are available so far about this enzyme. Genes coding for it were identified in Aquifex aeolicus, a Gram-negative, hyperthermophilic, chemolithoautotrophic and microaerophilic bacterium that uses inorganic sulfur compounds as electron donor to grow. We provide biochemical evidence that this Hdr-like enzyme is present in this sulfur-oxidizing prokaryote (cultivated with thiosulfate or elemental sulfur). We demonstrate, by immunolocalization and cell fractionation, that Hdr-like enzyme is associated, presumably monotopically, with the membrane fraction. We show by co-immunoprecipitation assay or partial purification, that the Hdr proteins form a stable complex composed of at least five subunits, HdrA, HdrB1, HdrB2, HdrC1 and HdrC2, present in two forms of high molecular mass on native gel (∼240 and 450 kDa). These studies allow us to propose a revised model for dissimilatory sulfur oxidation pathways in A. aeolicus, with Hdr predicted to generate sulfite. | 2016 |
Ehrenfeld N , Levicán, Gloria, Parada P . Heterodisulfide Reductase from Acidithiobacilli is a Key Component Involved in Metabolism of Reduced Inorganic Sulfur Compounds[J]. Advanced Materials Research, 2013, 825:194-197.