ArticleJournal of bacteriology2007
The pio operon is essential for phototrophic Fe(II) oxidation in Rhodopseudomonas palustris TIE-1.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.
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108 citing papers in PubMed.
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- Non-Respiratory Extracellular Electron Transfer Competes with Nitrogenase for Electrons in Rhodopseudomonas Palustris.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
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- Microbial electrosynthesis meets synthetic biology: Bioproduction from waste feedstocks.Biotechnology notes (Amsterdam, Netherlands) · 2025Review
- Biological and Chemical Processes of Nitrate Reduction and Ferrous Oxidation Mediated byMicroorganisms · 2024Article
- Elucidating metabolic tuning of mixed purple phototrophic bacteria biofilms in photoheterotrophic conditions through microbial photo-electrosynthesis.Communications biology · 2024Article
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- Large-scale prediction of outer-membrane multiheme cytochromes uncovers hidden diversity of electroactive bacteria and underlying pathways.Frontiers in microbiology · 2024Article
- Gallionellaceae pangenomic analysis reveals insight into phylogeny, metabolic flexibility, and iron oxidation mechanisms.mSystems · 2023Article
- Conductive proteins-based extracellular electron transfer of electroactive microorganisms.Quantitative biology (Beijing, China) · 2023Review
- Protein Interactions inMolecules (Basel, Switzerland) · 2023Article
48 more citing papers are in PubMed but not listed here.
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Abstract
Phototrophic Fe(II)-oxidizing bacteria couple the oxidation of ferrous iron [Fe(II)] to reductive CO(2) fixation by using light energy, but until recently, little has been understood about the molecular basis for this process. Here we report the discovery, with Rhodopseudomonas palustris TIE-1 as a model organism, of a three-gene operon, designated the pio operon (for phototrophic iron oxidation), that is necessary for phototrophic Fe(II) oxidation. The first gene in the operon, pioA, encodes a c-type cytochrome that is upregulated under Fe(II)-grown conditions. PioA contains a signal sequence and shares homology with MtrA, a decaheme c-type cytochrome from Shewanella oneidensis MR-1. The second gene, pioB, encodes a putative outer membrane beta-barrel protein. PioB is a homologue of MtrB from S. oneidensis MR-1. The third gene, pioC, encodes a putative high potential iron sulfur protein (HiPIP) with a twin-arginine translocation (Tat) signal sequence and is similar to the putative Fe(II) oxidoreductase (Iro) from Acidithiobacillus ferrooxidans. Like PioA, PioB and PioC appear to be secreted proteins. Deletion of the pio operon results in loss of Fe(II) oxidation activity and growth on Fe(II). Complementation studies confirm that the phenotype of this mutant is due to loss of the pio genes. Deletion of pioA alone results in loss of almost all Fe(II) oxidation activity; however, deletion of either pioB or pioC alone results in only partial loss of Fe(II) oxidation activity. Together, these results suggest that proteins encoded by the pio operon are essential and specific for phototrophic Fe(II) oxidation in R. palustris TIE-1.
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