{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T04:14:11Z","timestamp":1792815251305,"version":"4.5.0"},"reference-count":45,"publisher":"Springer Science and Business Media LLC","issue":"3","license":[{"start":{"date-parts":[[2026,8,8]],"date-time":"2026-08-08T00:00:00Z","timestamp":1786147200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2026,8,8]],"date-time":"2026-08-08T00:00:00Z","timestamp":1786147200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Planta"],"published-print":{"date-parts":[[2026,9]]},"DOI":"10.1007\/s00425-026-05122-8","type":"journal-article","created":{"date-parts":[[2026,8,8]],"date-time":"2026-08-08T14:01:07Z","timestamp":1786197667000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Vitamin K in photosynthetic organisms"],"prefix":"10.1007","volume":"264","author":[{"given":"Jerzy","family":"Kruk","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beatrycze","family":"Nowicka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Renata","family":"Szyma\u0144ska","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Micha\u0142","family":"Gabruk","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,8,8]]},"reference":[{"key":"5122_CR1","doi-asserted-by":"publisher","DOI":"10.3390\/nu12061852","volume":"12","author":"AC Akbulut","year":"2020","unstructured":"Akbulut AC, Pavlic A, Petsophonsakul P, Halder M, Maresz K, Kramann R, Schurgers L (2020) Vitamin K2 needs an RDI separate from vitamin K1. Nutrients 12:1852. https:\/\/doi.org\/10.3390\/nu12061852","journal-title":"Nutrients"},{"key":"5122_CR2","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1016\/S0021-9258(18)75069-2","volume":"111","author":"HJ Almquist","year":"1935","unstructured":"Almquist HJ, Stokstad ELR (1935) Hemorrhagic chick disease of dietary origin. J Biol Chem 111:105\u2013113. https:\/\/doi.org\/10.1016\/S0021-9258(18)75069-2","journal-title":"J Biol Chem"},{"key":"5122_CR3","doi-asserted-by":"publisher","first-page":"1028","DOI":"10.2174\/1389557516666160623082714","volume":"17","author":"J Basset","year":"2017","unstructured":"Basset J, Latimer GS, Fatihi A, Soubeyrand E, Block A (2017) Phylloquinone (vitamin K1): occurrence, biosynthesis and functions. Mini Rev Med Chem 17:1028\u20131038. https:\/\/doi.org\/10.2174\/1389557516666160623082714","journal-title":"Mini Rev Med Chem"},{"key":"5122_CR4","doi-asserted-by":"publisher","first-page":"807","DOI":"10.1007\/s00425-016-2643-y","volume":"245","author":"C Biniek","year":"2017","unstructured":"Biniek C, Heyno E, Kruk J, Sparla F, Trost P, Krieger-Liszkay A (2017) Role of the NAD(P)H quinone oxidoreductase NQR and the cytochrome b AIR12 in controlling superoxide generation at the plasma membrane. Planta 245:807\u2013817. https:\/\/doi.org\/10.1007\/s00425-016-2643-y","journal-title":"Planta"},{"key":"5122_CR5","doi-asserted-by":"publisher","first-page":"219","DOI":"10.1111\/j.1753-4887.1978.tb03688.x","volume":"130","author":"SB Binkley","year":"1939","unstructured":"Binkley SB, MacCorquodale DW, Thayer SA, Doisy EA (1939) The isolation of vitamin K1. J Biol Chem 130:219\u2013234. https:\/\/doi.org\/10.1111\/j.1753-4887.1978.tb03688.x","journal-title":"J Biol Chem"},{"key":"5122_CR6","doi-asserted-by":"publisher","first-page":"2768","DOI":"10.1128\/JB.00141-13","volume":"195","author":"M Chen","year":"2013","unstructured":"Chen M, Ma X, Chen X, Jiang M, Song H, Guo Z (2013) Identification of a hotdog fold thioesterase involved in the biosynthesis of menaquinone in Escherichia coli. J Bacteriol 195:2768\u20132775. https:\/\/doi.org\/10.1128\/JB.00141-13","journal-title":"J Bacteriol"},{"key":"5122_CR7","doi-asserted-by":"publisher","first-page":"1273","DOI":"10.1042\/bj0291273","volume":"29","author":"H Dam","year":"1935","unstructured":"Dam H (1935) The antihaemorrhagic vitamin of the chick. Biochem J 29:1273\u20131285. https:\/\/doi.org\/10.1042\/bj0291273","journal-title":"Biochem J"},{"key":"5122_CR8","doi-asserted-by":"publisher","DOI":"10.1007\/s11120-025-01180-3","volume":"163","author":"G Dickinson","year":"2025","unstructured":"Dickinson G, Stutts LR, Latimer S, Smith N, Batyrshina Z, Kula-Maximenko M, \u015alesak I, Block AK, Wilson MA, Basset GJ (2025) Quinol C-methyltransferases from extant species of early cyanobacterial lineages shed light on the emergence of plastoquinone in oxygenic phototrophs. Photosynth Res 163:59. https:\/\/doi.org\/10.1007\/s11120-025-01180-3","journal-title":"Photosynth Res"},{"key":"5122_CR9","doi-asserted-by":"publisher","first-page":"1730","DOI":"10.1105\/tpc.15.00103","volume":"27","author":"A Fatihi","year":"2015","unstructured":"Fatihi A, Latimer S, Schmollinger S, Block A, Dussault PH, Vermaas WF, Merchant SS, Basset GJ (2015) A dedicated type II NADPH dehydrogenase performs the penultimate step in the biosynthesis of vitamin K1 in Synechocystis and Arabidopsis. Plant Cell 27:1730\u20131741. https:\/\/doi.org\/10.1105\/tpc.15.00103","journal-title":"Plant Cell"},{"key":"5122_CR10","first-page":"2559","volume":"61","author":"LF Fieser","year":"1939","unstructured":"Fieser LF, Campbell WP, Fry EM, Gates MD Jr (1939) Synthetic approach to vitamin K1. J Am Chem Soc 61:2559","journal-title":"J Am Chem Soc"},{"key":"5122_CR11","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1111\/j.1365-313X.2010.04305.x","volume":"64","author":"F Furt","year":"2010","unstructured":"Furt F, Oostende CV, Widhalm JR, Dale MA, Wertz J, Basset GJ (2010) A bimodular oxidoreductase mediates the specific reduction of phylloquinone (vitamin K1) in chloroplasts. Plant J 64:38\u201346. https:\/\/doi.org\/10.1111\/j.1365-313X.2010.04305.x","journal-title":"Plant J"},{"key":"5122_CR12","doi-asserted-by":"publisher","first-page":"3669","DOI":"10.1093\/jxb\/ert203","volume":"64","author":"P Gawro\u0144ski","year":"2013","unstructured":"Gawro\u0144ski P, G\u00f3recka M, Bederska M, Rusaczonek A, \u015alesak I, Kruk J, Karpi\u0144ski S (2013) Isochorismate synthase 1 is required for thylakoid organization, optimal plastoquinone redox status and state transitions in Arabidopsis thaliana. J Exp Bot 64:3669\u20133679. https:\/\/doi.org\/10.1093\/jxb\/ert203","journal-title":"J Exp Bot"},{"key":"5122_CR13","doi-asserted-by":"publisher","first-page":"17189","DOI":"10.1074\/jbc.M601754200","volume":"281","author":"J Gross","year":"2006","unstructured":"Gross J, Cho WK, Lezhneva L, Falk J, Krupinska K, Shinozaki K, Seki M, Herrmann RG, Meurer J (2006) A plant locus essential for phylloquinone (vitamin K1) biosynthesis originated from a fusion of four eubacterial genes. J Biol Chem 281:17189\u201317196. https:\/\/doi.org\/10.1074\/jbc.M601754200","journal-title":"J Biol Chem"},{"key":"5122_CR14","doi-asserted-by":"publisher","first-page":"1976546","DOI":"10.1080\/15592324.2021.1976546","volume":"16","author":"X Gu","year":"2021","unstructured":"Gu X, Chen IG, Tsai CJ (2021a) How do holoparasitic plants exploit vitamin K1? Plant Sigal Behav 16:1976546. https:\/\/doi.org\/10.1080\/15592324.2021.1976546","journal-title":"Plant Sigal Behav"},{"key":"5122_CR15","doi-asserted-by":"publisher","first-page":"1443","DOI":"10.1093\/plphys\/kiab031","volume":"185","author":"X Gu","year":"2021","unstructured":"Gu X, Chen IG, Harding SA, Nyamdari B, Ortega MA, Clermont K, Westwood JH, Tsai CJ (2021b) Plasma membrane phylloquinone biosynthesis in nonphotosynthetic parasitic plants. Plant Physiol 185:1443\u20131456. https:\/\/doi.org\/10.1093\/plphys\/kiab031","journal-title":"Plant Physiol"},{"key":"5122_CR16","doi-asserted-by":"publisher","first-page":"4437","DOI":"10.1073\/pnas.081078898","volume":"98","author":"M Guergova-Kuras","year":"2001","unstructured":"Guergova-Kuras M, Boudreaux B, Joliot A, Joliot P, Redding K (2001) Evidence for two active branches for electron transfer in photosystem I. Proc Natl Acad Sci U S A 98:4437\u20134442. https:\/\/doi.org\/10.1073\/pnas.081078898","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5122_CR17","doi-asserted-by":"publisher","first-page":"351","DOI":"10.1016\/j.bbabio.2008.01.011","volume":"1777","author":"Y Ikeda","year":"2008","unstructured":"Ikeda Y, Komura M, Watanabe M, Minami C, Koike H, Itoh S, Kashino Y, Satoh K (2008) Photosystem I complexes associated with fucoxanthin-chlorophyll-binding proteins from a marine centric diatom, Chaetoceros gracilis. Biochim Biophys Acta 1777:351\u2013361. https:\/\/doi.org\/10.1016\/j.bbabio.2008.01.011","journal-title":"Biochim Biophys Acta"},{"key":"5122_CR18","doi-asserted-by":"publisher","first-page":"520","DOI":"10.1016\/j.bbamcr.2007.11.006","volume":"1783","author":"K Inaba","year":"2008","unstructured":"Inaba K, Ito K (2008) Structure and mechanisms of the DsbB\u2013DsbA disulfide bond generation machine. Biochim Biophys Acta 1783:520\u2013529. https:\/\/doi.org\/10.1016\/j.bbamcr.2007.11.006","journal-title":"Biochim Biophys Acta"},{"key":"5122_CR19","doi-asserted-by":"publisher","first-page":"4462","DOI":"10.1105\/tpc.111.089680","volume":"23","author":"M Karamoko","year":"2011","unstructured":"Karamoko M, Cline S, Redding K, Ruiz N, Hamel PP (2011) Lumen Thiol Oxidoreductase1, a disulfide bond-forming catalyst, is required for the assembly of photosystem II in Arabidopsis. Plant Cell 23:4462\u20134475. https:\/\/doi.org\/10.1105\/tpc.111.089680","journal-title":"Plant Cell"},{"key":"5122_CR20","doi-asserted-by":"publisher","first-page":"4364","DOI":"10.1016\/j.febslet.2014.10.003","volume":"588","author":"MA Kozuleva","year":"2014","unstructured":"Kozuleva MA, Petrova AA, Mamedov MD, Semenov AY, Ivanov BN (2014) O2 reduction by photosystem I involves phylloquinone under steady-state illumination. FEBS Lett 588:4364\u20134368. https:\/\/doi.org\/10.1016\/j.febslet.2014.10.003","journal-title":"FEBS Lett"},{"key":"5122_CR21","doi-asserted-by":"publisher","first-page":"1848","DOI":"10.1093\/plphys\/kiab221","volume":"186","author":"M Kozuleva","year":"2021","unstructured":"Kozuleva M, Petrova A, Milrad Y, Semenov A, Ivanov B, Redding KE, Yacoby I (2021) Phylloquinone is the principal Mehler reaction site within photosystem I in high light. Plant Physiol 186:1848\u20131858. https:\/\/doi.org\/10.1093\/plphys\/kiab221","journal-title":"Plant Physiol"},{"key":"5122_CR22","doi-asserted-by":"publisher","first-page":"8501","DOI":"10.1021\/bi034036q","volume":"42","author":"J Kruk","year":"2003","unstructured":"Kruk J, Jemio\u0142a-Rzemi\u0144ska M, Burda K, Schmid GH, Strza\u0142ka K (2003) Scavenging of superoxide generated in photosystem I by plastoquinol and other prenyllipids in thylakoid membranes. Biochemistry 42:8501\u20138505. https:\/\/doi.org\/10.1021\/bi034036q","journal-title":"Biochemistry"},{"key":"5122_CR23","doi-asserted-by":"publisher","first-page":"507","DOI":"10.1016\/j.devcel.2016.10.012","volume":"463","author":"W Li","year":"2010","unstructured":"Li W, Schulman S, Dutton RJ, Boyd D, Beckwith J, Rapoport TA (2010) Structure of a bacterial homologue of vitamin K epoxide reductase. Nature 463:507\u2013512. https:\/\/doi.org\/10.1016\/j.devcel.2016.10.012","journal-title":"Nature"},{"key":"5122_CR24","doi-asserted-by":"publisher","first-page":"508","DOI":"10.1016\/j.devcel.2016.10.012","volume":"39","author":"S Li","year":"2016","unstructured":"Li S, Yamada M, Han X, Ohler U, Benfey PN (2016) High-resolution expression map of the Arabidopsis root reveals alternative splicing and lincRNA regulation. Dev Cell 39:508\u2013522","journal-title":"Dev Cell"},{"key":"5122_CR25","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1002\/biof.5520180209","volume":"18","author":"K Lochner","year":"2003","unstructured":"Lochner K, D\u00f6ring O, B\u00f6ttger M (2003) Phylloquinone, what can we learn from plants? BioFactors 18:73\u201378. https:\/\/doi.org\/10.1002\/biof.5520180209","journal-title":"BioFactors"},{"key":"5122_CR26","doi-asserted-by":"publisher","first-page":"1427","DOI":"10.1007\/s00299-013-1455-9","volume":"32","author":"Y Lu","year":"2013","unstructured":"Lu Y, Wang HR, Li H, Cui HR, Feng YG, Wang XY (2013) A chloroplast membrane protein LTO1\/AtVKOR involving in redox regulation and ROS homeostasis. Plant Cell Rep 32:1427\u20131440. https:\/\/doi.org\/10.1007\/s00299-013-1455-9","journal-title":"Plant Cell Rep"},{"key":"5122_CR27","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1007\/BF01279292","volume":"205","author":"S L\u00fcthje","year":"1998","unstructured":"L\u00fcthje S, Van Gestelen P, Cordoba-Pedregosa MC, Gonzalez-Reyes JA, Asard H, Villalba JM, B\u00f6ttger M (1998) Quinones in plant plasma membranes \u2013 a missing link? Protoplasma 205:43\u201351. https:\/\/doi.org\/10.1007\/BF01279292","journal-title":"Protoplasma"},{"key":"5122_CR28","doi-asserted-by":"publisher","first-page":"3493","DOI":"10.1016\/j.febslet.2005.05.029","volume":"579","author":"M Mimuro","year":"2005","unstructured":"Mimuro M, Tsuchiya T, Inoue H, Sakuragi Y, Itoh Y, Gotoh T, Miyashita H, Bryant DA, Kobayashi M (2005) The secondary electron acceptor of photosystem I in Gloeobacter violaceus PCC 7421 is menaquinone-4 that is synthesized by a unique but unknown pathway. FEBS Lett 579:3493\u20133496. https:\/\/doi.org\/10.1016\/j.febslet.2005.05.029","journal-title":"FEBS Lett"},{"key":"5122_CR29","doi-asserted-by":"publisher","first-page":"1587","DOI":"10.1016\/j.bbabio.2010.06.007","volume":"1797","author":"B Nowicka","year":"2010","unstructured":"Nowicka B, Kruk J (2010) Occurrence, biosynthesis and function of isoprenoid quinones. Biochimica Et Biophysica Acta (BBA) - Bioenergetics 1797:1587\u20131605. https:\/\/doi.org\/10.1016\/j.bbabio.2010.06.007","journal-title":"Biochimica Et Biophysica Acta (BBA) - Bioenergetics"},{"key":"5122_CR30","doi-asserted-by":"publisher","first-page":"2457","DOI":"10.1016\/j.phytochem.2008.07.006","volume":"69","author":"C Oostende","year":"2008","unstructured":"Oostende C, Widhalm JR, Basset GJC (2008) Detection and quantification of vitamin K1 quinol in leaf tissues. Phytochemistry 69:2457\u20132462. https:\/\/doi.org\/10.1016\/j.phytochem.2008.07.006","journal-title":"Phytochemistry"},{"key":"5122_CR31","doi-asserted-by":"publisher","first-page":"230","DOI":"10.1016\/B978-0-12-385853-5.00001-5","volume":"59","author":"C Oostende","year":"2011","unstructured":"Oostende C, Widhalm JR, Furt F, Ducluzeau AL, Basset GJ (2011) Vitamin K1 (phylloquinone): function, enzymes and genes. Adv Bot Res 59:230\u2013255. https:\/\/doi.org\/10.1016\/B978-0-12-385853-5.00001-5","journal-title":"Adv Bot Res"},{"key":"5122_CR32","doi-asserted-by":"publisher","DOI":"10.3389\/fnut.2021.753059","volume":"8","author":"CR Palmer","year":"2021","unstructured":"Palmer CR, Koch H, Shinde S, Blekkenhorst LC, Lewis JR, Croft KD, Hodgson JM, Sim M (2021) Development of a vitamin K database for commercially available food in Australia. Front Nutr 8:753059. https:\/\/doi.org\/10.3389\/fnut.2021.753059","journal-title":"Front Nutr"},{"key":"5122_CR33","doi-asserted-by":"publisher","first-page":"14354","DOI":"10.1073\/pnas.1104790108","volume":"108","author":"LE Piller","year":"2011","unstructured":"Piller LE, Besagni C, Ksas B, Rumeau D, Brehelin C, Glauser G, Kessler F, Havaux M (2011) Chloroplast lipid droplet type II NAD(P)H quinone oxidoreductase is essential for prenylquinone metabolism and vitamin K1 accumulation. Proc Natl Acad Sci USA 108:14354\u201314359. https:\/\/doi.org\/10.1073\/pnas.1104790108","journal-title":"Proc Natl Acad Sci USA"},{"key":"5122_CR34","doi-asserted-by":"publisher","first-page":"606","DOI":"10.1104\/pp.109.139170","volume":"150","author":"V Preger","year":"2009","unstructured":"Preger V, Tango N, Marchand C, Lemaire SD, Carbonera D, DiValentin M, Costa A, Pupillo P, Trost P (2009) Auxin-responsive genes AIR12 code for a new family of plasma membrane b-type cytochromes specific to flowering plants. Plant Physiol 150:606\u2013620. https:\/\/doi.org\/10.1104\/pp.109.139170","journal-title":"Plant Physiol"},{"key":"5122_CR35","doi-asserted-by":"publisher","first-page":"12371","DOI":"10.1074\/jbc.M412943200","volume":"280","author":"Y Sakuragi","year":"2005","unstructured":"Sakuragi Y, Zybailov B, Shen G, Bryant DA, Golbeck JH, Diner BA, Karygina I, Pushkar Y, Stehlik D (2005) Recruitment of a foreign quinone into the A1 site of photosystem I. Characterization of a menBrubA double deletion mutant in Synechococcus sp. PCC 7002 devoid of FX, FA, and FB and containing plastoquinone or exchanged 9,10-anthraquinone. J Biol Chem 280:12371\u201312381. https:\/\/doi.org\/10.1074\/jbc.M412943200","journal-title":"J Biol Chem"},{"key":"5122_CR36","doi-asserted-by":"publisher","first-page":"15762","DOI":"10.1074\/jbc.M800982200","volume":"283","author":"AK Singh","year":"2008","unstructured":"Singh AK, Bhattacharyya-Pakrasi M, Pakrasi HB (2008) Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organisms. J Biol Chem 283:15762\u201315770. https:\/\/doi.org\/10.1074\/jbc.M800982200","journal-title":"J Biol Chem"},{"key":"5122_CR37","doi-asserted-by":"publisher","first-page":"21740","DOI":"10.1074\/jbc.M116.732545","volume":"291","author":"SK Singh","year":"2016","unstructured":"Singh SK, Hasan SS, Zakharov SD, Naurin S, Cohn W, Ma J, Whitelegge JP, Cramer WA (2016) Transmembrane signaling in photosynthetic state transitions: redox- and structure-dependent interaction in vitro between Stt7 kinase and the cytochrome b6f complex. J Biol Chem 291:21740\u201321750. https:\/\/doi.org\/10.1074\/jbc.M116.732545","journal-title":"J Biol Chem"},{"key":"5122_CR38","doi-asserted-by":"publisher","first-page":"3686","DOI":"10.1093\/plcell\/koad202","volume":"35","author":"L Stutts","year":"2023","unstructured":"Stutts L, Latimer S, Batyrshina Z, Dickinson G, Alborn H, Block AK, Basset GJ (2023) The evolution of strictly monofunctional naphthoquinol C-methyltransferases is vital in cyanobacteria and plastids. Plant Cell 35:3686\u20133696. https:\/\/doi.org\/10.1093\/plcell\/koad202","journal-title":"Plant Cell"},{"key":"5122_CR39","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1016\/B978-0-12-378630-2.00095-5","volume-title":"Encyclopedia of biological chemistry","author":"JW Suttie","year":"2013","unstructured":"Suttie JW (2013) Vitamin K: biochemistry, metabolism, and nutritional aspects. In: Lennarz WJ, Lane MD (eds) Encyclopedia of biological chemistry, 2nd Ed. Elsevier Inc., Amsterdam, The Netherlands, pp 551\u2013554","edition":"2nd Ed"},{"key":"5122_CR40","doi-asserted-by":"publisher","first-page":"808","DOI":"10.1038\/s41586-024-08484-9","volume":"639","author":"R Wang","year":"2025","unstructured":"Wang R, Chen B, Elghobashi-Meinhardt N, Tie JK, Ayala A, Zhou N, Qi X (2025) Structure and mechanism of vitamin-K dependent \u03b3-glutamyl carboxylase. Nature 639:808\u2013815. https:\/\/doi.org\/10.1038\/s41586-024-08484-9","journal-title":"Nature"},{"key":"5122_CR41","doi-asserted-by":"publisher","first-page":"5599","DOI":"10.1073\/pnas.0900738106","volume":"106","author":"JR Widhalm","year":"2009","unstructured":"Widhalm JR, van Oostende C, Furt F, Basset GJC (2009) A dedicated thioesterase of the hotdog-fold family is required for the biosynthesis of the naphthoquinone ring of vitamin K1. Proc Natl Acad Sci U S A 106:5599\u20135603. https:\/\/doi.org\/10.1073\/pnas.0900738106","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5122_CR42","doi-asserted-by":"publisher","first-page":"205","DOI":"10.1111\/j.1365-313X.2012.04972.x","volume":"71","author":"JR Widhalm","year":"2012","unstructured":"Widhalm JR, Ducluzeau AL, Buller NE, Elowsky CG, Olsen LJ, Basset GJC (2012) Phylloquinone (vitamin K1) biosynthesis in plants: two peroxisomal thioesterases of lactobacillales origin hydrolyze 1,4-dihydroxy-2-naphthoyl-CoA. Plant J 71:205\u2013215. https:\/\/doi.org\/10.1111\/j.1365-313X.2012.04972.x","journal-title":"Plant J"},{"key":"5122_CR43","doi-asserted-by":"publisher","first-page":"964","DOI":"10.1093\/plphys\/kiab267","volume":"186","author":"J Wu","year":"2021","unstructured":"Wu J, Rong L, Lin W, Kong L, Wei D, Zhang L, Rochaix JD, Xu X (2021) Functional redox links between lumen thiol oxidoreductase1 and serine\/threonine-protein kinase STN7. Plant Physiol 186:964\u2013976. https:\/\/doi.org\/10.1093\/plphys\/kiab267","journal-title":"Plant Physiol"},{"key":"5122_CR44","doi-asserted-by":"publisher","first-page":"1001","DOI":"10.2116\/analsci.19.1001","volume":"19","author":"E Yoshida","year":"2003","unstructured":"Yoshida E, Nakamura A, Watanabe T (2003) Reversed-phase HPLC determination of chlorophyll a\u2019 and naphthoquinones in photosystem I of red algae: existence of two menaquinone-4 molecules in photosystem I of Cyanidium caldarium. Anal Sci 19:1001\u20131005. https:\/\/doi.org\/10.2116\/analsci.19.1001","journal-title":"Anal Sci"},{"key":"5122_CR45","doi-asserted-by":"publisher","first-page":"468","DOI":"10.1515\/znc-1989-5-621","volume":"44","author":"K Ziegler","year":"1989","unstructured":"Ziegler K, Maldene I, Lockau W (1989) 5\u2019-Monohydroxyphylloquinone as a component of photosystem I. Z Naturforsch C 44:468\u2013472","journal-title":"Z Naturforsch C"}],"container-title":["Planta"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00425-026-05122-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s00425-026-05122-8","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00425-026-05122-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T15:43:09Z","timestamp":1786722189000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s00425-026-05122-8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,8]]},"references-count":45,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2026,9]]}},"alternative-id":["5122"],"URL":"https:\/\/doi.org\/10.1007\/s00425-026-05122-8","relation":{},"ISSN":["0032-0935","1432-2048"],"issn-type":[{"value":"0032-0935","type":"print"},{"value":"1432-2048","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,8]]},"assertion":[{"value":"13 May 2026","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"2 August 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"8 August 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare that there is no conflict of interest.","order":1,"name":"Ethics","label":"Conflict of interest","group":{"name":"EthicsHeading","label":"Declarations"}}],"article-number":"91"}}