ArticleCurrent microbiology2010
Bacteriophytochrome-dependent regulation of light-harvesting complexes in Rhodopseudomonas palustris anaerobic cultures.
Article in Current microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 10 citations in OpenAlex.
- Article
- Membrane-Bound Bacteriophytochrome-Like Complex of Phototrophic Purple Non-Sulfur Bacterium Rhodopseudomonas palustris.Doklady. Biochemistry and biophysics · 2018Article
- Apo-bacteriophytochromes modulate bacterial photosynthesis in response to low light.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Revealing the functions of the transketolase enzyme isoforms in Rhodopseudomonas palustris using a systems biology approach.PloS one · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteriophytochromes (Bphs) are photoreceptors that help bacteria sense changes in light wavelength and intensity. Bphs contain a linear tetrapyrrole chromophore that, upon absorption of red or far-red light, undergoes a cis-trans isomerization that leads to a conformational change in the holoprotein. The conformation and type of Bph affects the expression of genes. The linear tetrapyrrole bound by Bphs is thought to come from O(2)-dependent cleavage of heme by a heme oxygenase. We have discovered that the absence of O(2) does not inhibit the normal function of two Bphs in the regulation of Rhodopseudomonas palustris light-harvesting complexes. These observations imply that: (i) a linear tetrapyrrole can be made anaerobically, either through anaerobic heme cleavage by a novel enzyme or directly from the heme precursor hydroxymethylbilane without ring cleavage; or (ii) that Bph-dependent signal transduction does not require a chromophore.
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Registered trials
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