{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T08:59:32Z","timestamp":1790672372578,"version":"4.1.0"},"reference-count":91,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T00:00:00Z","timestamp":1790640000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T00:00:00Z","timestamp":1790640000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100002347","name":"Bundesministerium f\u00fcr Bildung und Forschung","doi-asserted-by":"publisher","award":["03SF0652A"],"award-info":[{"award-number":["03SF0652A"]}],"id":[{"id":"10.13039\/501100002347","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000015","name":"U.S. Department of Energy","doi-asserted-by":"publisher","award":["DE\u2010AC36\u201008GO28308"],"award-info":[{"award-number":["DE\u2010AC36\u201008GO28308"]}],"id":[{"id":"10.13039\/100000015","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005941","name":"Dietmar Hopp Stiftung","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005941","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"abstract":"<jats:p>\n                    Ferredoxins are central to cellular metabolism by mediating electron flow in energy conversion reactions. The focus of this study was to systematically examine twelve ferredoxin and ferredoxin\u2010like proteins from\n                    <jats:italic>Synechocystis<\/jats:italic>\n                    sp. PCC 6803 to identify their properties, activities, and functions in electron transfer. Using electron paramagnetic resonance spectroscopy, we detected cluster types consistent with major ferredoxin families including plant\u2010type [2Fe\u20102S], adrenodoxin, thioredoxin, and bacterial\u2010type [4Fe\u20104S] ferredoxins. In addition, we found that the ssr3184 ferredoxin\u2010like protein exchanged between a [3Fe\u20104S] or a [4Fe\u20104S] cluster, pointing to a possible functional change in response to changes in oxygen or cellular redox poise. Electrochemical measurements demonstrated that these ferredoxins constitute a broad potential window, from \u2212243\u2009mV to \u2212520\u2009mV vs SHE. Investigations on their capacity to support electron transfer focused on reactions with two major redox hubs: Photosystem I and pyruvate:ferredoxin oxidoreductase and included testing of binding interactions with nitrite reductase. Expression profiling under multiple environmental conditions was also used to predict function and revealed distinct regulatory patterns. Collectively, these findings identified a group of core ferredoxins that directly support photosynthetic electron transfer, and more specialized ones that may serve other functions. In summary,\n                    <jats:italic>Synechocystis<\/jats:italic>\n                    utilizes a suite of ferredoxins to maintain cellular redox homeostasis under dynamic environmental conditions.\n                  <\/jats:p>","DOI":"10.1111\/febs.70728","type":"journal-article","created":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T08:03:46Z","timestamp":1790669026000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["A comprehensive study on ferredoxin isoforms in the cyanobacterium Synechocystis sp.\n                    <scp>PCC<\/scp>\n                    6803"],"prefix":"10.1111","author":[{"given":"Marko","family":"Boehm","sequence":"first","affiliation":[{"name":"Department of Biology, Botanical Institute Christian\u2010Albrechts\u2010University  Kiel Germany"},{"name":"Department of Molecular Plant Physiology, Bioenergetics in Photoautotrophs University of Kassel  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Drazenka","family":"Svedruzic","sequence":"additional","affiliation":[{"name":"National Laboratory of the Rockies Biosciences Center  Golden Colorado USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carolyn E.","family":"Lubner","sequence":"additional","affiliation":[{"name":"National Laboratory of the Rockies Biosciences Center  Golden Colorado USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jens","family":"Appel","sequence":"additional","affiliation":[{"name":"Department of Biology, Botanical Institute Christian\u2010Albrechts\u2010University  Kiel Germany"},{"name":"Department of Molecular Plant Physiology, Bioenergetics in Photoautotrophs University of Kassel  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David W.","family":"Mulder","sequence":"additional","affiliation":[{"name":"National Laboratory of the Rockies Biosciences Center  Golden Colorado USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1842-5691","authenticated-orcid":false,"given":"Effie C.","family":"Kisgeropoulos","sequence":"additional","affiliation":[{"name":"National Laboratory of the Rockies Biosciences Center  Golden Colorado USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vanessa","family":"Hueren","sequence":"additional","affiliation":[{"name":"Department of Biology, Botanical Institute Christian\u2010Albrechts\u2010University  Kiel Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katharina","family":"Spengler","sequence":"additional","affiliation":[{"name":"Department of Biology, Botanical Institute Christian\u2010Albrechts\u2010University  Kiel Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vivek S.","family":"Bharadwaj","sequence":"additional","affiliation":[{"name":"National Laboratory of the Rockies Biosciences Center  Golden Colorado USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhanjun","family":"Guo","sequence":"additional","affiliation":[{"name":"National Laboratory of the Rockies Biosciences Center  Golden Colorado USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anastasia E.","family":"Ledinina","sequence":"additional","affiliation":[{"name":"National Laboratory of the Rockies Biosciences Center  Golden Colorado USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Darja","family":"Deobald","sequence":"additional","affiliation":[{"name":"Department Environmental Molecular Biotechnology Helmholtz Centre for Environmental Research \u2013 UFZ  Leipzig Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lorenz","family":"Adrian","sequence":"additional","affiliation":[{"name":"Department Environmental Molecular Biotechnology Helmholtz Centre for Environmental Research \u2013 UFZ  Leipzig Germany"},{"name":"Chair of Geobiotechnology Technical University Berlin  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5039-654X","authenticated-orcid":false,"given":"Paul W.","family":"King","sequence":"additional","affiliation":[{"name":"National Laboratory of the Rockies Biosciences Center  Golden Colorado USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4366-423X","authenticated-orcid":false,"given":"Kirstin","family":"Gutekunst","sequence":"additional","affiliation":[{"name":"Department of Biology, Botanical Institute Christian\u2010Albrechts\u2010University  Kiel Germany"},{"name":"Department of Molecular Plant Physiology, Bioenergetics in Photoautotrophs University of Kassel  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,9,29]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1002463","article-title":"Energetic selection of topology in ferredoxins","volume":"8","author":"Kim JD","year":"2012","journal-title":"PLoS Comput Biol"},{"key":"e_1_2_10_3_1","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1007\/s00775-007-0318-7","article-title":"Iron\u2013sulfur protein folds, iron\u2013sulfur chemistry, and evolution","volume":"13","author":"Meyer J","year":"2008","journal-title":"J Biol Inorg Chem"},{"key":"e_1_2_10_4_1","doi-asserted-by":"crossref","first-page":"4366","DOI":"10.1021\/cr400479b","article-title":"Metalloproteins containing cytochrome, iron\u2013sulfur, or copper redox centers","volume":"114","author":"Liu J","year":"2014","journal-title":"Chem 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