Disease relevance of Rhodovulum

• Rhodovulum iodosum sp. nov. and Rhodovulum robiginosum sp. nov., two new marine phototrophic ferrous-iron-oxidizing purple bacteria [1].
• Taking the morphology, photosynthetic pigments, aerobic growth in the dark, and utilization of sulfide for phototrophic growth into account, strain SiCys was assigned to the genus Rhodovulum (formerly Rhodobacter) and tentatively classified as a strain of R. sulfidophilum [2].

High impact information on Rhodovulum

• The g-tensor orientation of the chemically reduced Rieske cluster in cytochrome bc(1) complex from Rhodovulum sulfidophilum with respect to the membrane was determined in the presence and absence of inhibitors and in the presence of oxidized and reduced quinone in the quinol-oxidizing-site (Q(o)-site) by EPR on two-dimensionally ordered samples [3].
• Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin-containing enzymes [4].
• Dimethyl sulfide dehydrogenase from the purple phototrophic bacterium Rhodovulum sulfidophilum catalyzes the oxidation of dimethyl sulfide to dimethyl sulfoxide [5].
• Characterization of the redox centers in dimethyl sulfide dehydrogenase from Rhodovulum sulfidophilum [5].
• Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum [6].

Chemical compound and disease context of Rhodovulum

• The SoxAX complex of the bacterium Rhodovulum sulfidophilum is a heterodimeric c-type cytochrome that plays an essential role in photosynthetic thiosulfate and sulfide oxidation [6].
• Like all known Rhodovulum species, the new strains had ovoid to rod-shaped cells, contained bacteriochlorophyll a and carotenoids of the spheroidene series, and were able to oxidize sulfide and thiosulfate [1].
• In contrast to the new strains, none of the known Rhodovulum species tested was able to oxidize ferrous iron or iron sulfide [1].
• Like Rhodovulum adriaticum, both strains were unable to assimilate sulfate; for growth they needed a reduced sulfur source, e.g. thiosulfate [1].
• Maximization of hydrogen production ability in high-density suspension of Rhodovulum sulfidophilum cells using intracellular poly(3-hydroxybutyrate) as sole substrate [7].

Biological context of Rhodovulum

• The cytochrome bc1 complex from Rhodovulum sulfidophilum purifies as a four-subunit complex: the cytochrome b, cytochrome c1 and Rieske iron-sulphur proteins, which are encoded together in the fbc operon, as well as a 6-kDa protein [8].
• An alternative to the accepted phylogeny of purple bacteria based on 16S rRNA: analyses of the amino acid sequences of cytochromes C2 and C556 from Rhodobacter (Rhodovulum) sulfidophilus [9].

Gene context of Rhodovulum

• A Rhodovulum sulfidophilum mutant lacking regA or regB was constructed [10].
• A thiosulfate-induced cytochrome c has been purified from the photosynthetic alpha-proteobacterium Rhodovulum sulfidophilum [11].
• SoxV, an orthologue of the CcdA disulfide transporter, is involved in thiosulfate oxidation in Rhodovulum sulfidophilum and reduces the periplasmic thioredoxin SoxW [12].

References