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The draft genome of the isolate encodes all of the enzymatic machinery necessary for both oxygenic and anoxygenic photosynthesis, as well as genes for methylating hopanoids at the C-2 position. The physiological response of the isolate to H2S is complex: (i) no induction time is necessary for anoxygenic photosynthesis; (ii) rates of anoxygenic photosynthesis are regulated by both H2S and irradiance; (iii) O2 production is inhibited by H2S concentrations as low as 1 \u00b5m and the recovery rate of oxygenic photosynthesis is dependent on irradiance; (iv) under the optimal light conditions for oxygenic photosynthesis, rates of anoxygenic photosynthesis are nearly double those of oxygenic photosynthesis. We hypothesize that the specific adaptation mechanisms of the isolate to H2S emerged from a close spatial interaction with sulfate-reducing bacteria. The new isolate, Leptolyngbya sp. strain hensonii, is not closely related to other well-characterized Cyanobacteria that can perform anoxygenic photosynthesis, which further highlights the need to characterize the diversity and biogeography of metabolically versatile Cyanobacteria. The isolate will be an ideal model organism for exploring the adaptation of Cyanobacteria to sulfidic conditions.<\/jats:p>","DOI":"10.1038\/ismej.2017.193","type":"journal-article","created":{"date-parts":[[2018,1,12]],"date-time":"2018-01-12T15:01:04Z","timestamp":1515769264000},"page":"568-584","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":67,"title":["Cyanobacterial photosynthesis under sulfidic conditions: insights from the isolate <i>Leptolyngbya<\/i> sp. strain hensonii"],"prefix":"10.1093","volume":"12","author":[{"given":"Trinity L","family":"Hamilton","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, University of Cincinnati , Cincinnati, OH 45221, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Judith M","family":"Klatt","sequence":"additional","affiliation":[{"name":"Max-Planck Institute for Marine Microbiology , Bremen, Germany"},{"name":"Geomicrobiology Lab, Department of Earth and Environmental Sciences, University of Michigan , Ann Arbor, MI, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5274-1781","authenticated-orcid":false,"given":"Dirk","family":"de Beer","sequence":"additional","affiliation":[{"name":"Max-Planck Institute for Marine Microbiology , Bremen, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jennifer L","family":"Macalady","sequence":"additional","affiliation":[{"name":"Department of Geosciences and the Penn State Astrobiology Research Center (PSARC), Pennsylvania State University , University Park, PA 16802, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2018,1,12]]},"reference":[{"key":"2024011609341283100_CR1","doi-asserted-by":"publisher","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","article-title":"Gapped BLAST and PSI-BLAST: a new generation of protein database search programs","volume":"25","author":"Altschul","year":"1997","journal-title":"Nucleic Acids Res"},{"key":"2024011609341283100_CR2","doi-asserted-by":"publisher","first-page":"1744","DOI":"10.1093\/pcp\/pcr108","article-title":"A heme oxygenase isoform is essential for aerobic growth in the cyanobacterium Synechocystis sp. 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