{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T14:53:13Z","timestamp":1761663193811},"reference-count":49,"publisher":"Springer Science and Business Media LLC","issue":"3","license":[{"start":{"date-parts":[[2013,9,7]],"date-time":"2013-09-07T00:00:00Z","timestamp":1378512000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Photosynth Res"],"published-print":{"date-parts":[[2013,12]]},"DOI":"10.1007\/s11120-013-9916-0","type":"journal-article","created":{"date-parts":[[2013,9,6]],"date-time":"2013-09-06T16:29:40Z","timestamp":1378484980000},"page":"209-218","source":"Crossref","is-referenced-by-count":11,"title":["Substitutions at the opening of the Rubisco central solvent channel affect holoenzyme stability and CO2\/O2 specificity but not activation by Rubisco activase"],"prefix":"10.1007","volume":"118","author":[{"given":"M. Gloria","family":"Esquivel","sequence":"first","affiliation":[]},{"given":"Todor","family":"Genkov","sequence":"additional","affiliation":[]},{"given":"Ana S.","family":"Nogueira","sequence":"additional","affiliation":[]},{"given":"Michael E.","family":"Salvucci","sequence":"additional","affiliation":[]},{"given":"Robert J.","family":"Spreitzer","sequence":"additional","affiliation":[]}],"member":"297","published-online":{"date-parts":[[2013,9,7]]},"reference":[{"key":"9916_CR1","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1006\/jmbi.1996.0310","volume":"259","author":"I Andersson","year":"1996","unstructured":"Andersson I (1996) Large structures at high resolution: the 1.6\u00a0\u00c5 crystal structure of spinach ribulose-1,5-bisphosphate carboxylase\/oxygenase complexed with 2-carboxyarabinitol bisphosphate. J Mol Biol 259:160\u2013174","journal-title":"J Mol Biol"},{"key":"9916_CR2","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.plaphy.2008.01.001","volume":"46","author":"I Andersson","year":"2008","unstructured":"Andersson I, Backlund A (2008) Structure and function of Rubisco. Plant Physiol Biochem 46:275\u2013291","journal-title":"Plant Physiol Biochem"},{"key":"9916_CR3","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/S0003-9861(03)00164-4","volume":"414","author":"I Andersson","year":"2003","unstructured":"Andersson I, Taylor TC (2003) Structural framework for catalysis and regulation in ribulose-1,5-bisphosphate carboxylase\/oxygenase. Arch Biochem Biophys 414:130\u2013140","journal-title":"Arch Biochem Biophys"},{"key":"9916_CR4","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1007\/978-1-60761-925-3_28","volume-title":"Photosynthesis research protocols, methods in molecular biology","author":"C Barta","year":"2011","unstructured":"Barta C, Carmo-Silva AE, Salvucci ME (2011a) Purification of Rubisco activase from leaves or after expression in Escherichia coli. In: Carpentier R (ed) Photosynthesis research protocols, methods in molecular biology, vol 684. Human Press, New York, pp 363\u2013374"},{"key":"9916_CR5","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1007\/978-1-60761-925-3_29","volume-title":"Photosynthesis research protocols, methods in molecular biology","author":"C Barta","year":"2011","unstructured":"Barta C, Carmo-Silva AE, Salvucci ME (2011b) Rubisco activase activity assays. In: Carpentier R (ed) Photosynthesis research protocols, methods in molecular biology, vol 684. Human Press, New York, pp 375\u2013382"},{"key":"9916_CR6","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1016\/0006-291X(71)90475-X","volume":"45","author":"G Bowes","year":"1971","unstructured":"Bowes G, Ogren WL, Hageman RH (1971) Phosphoglycolate production catalyzed by ribulose diphosphate carboxylase. Biochem Biophys Res Commun 45:716\u2013722","journal-title":"Biochem Biophys Res Commun"},{"key":"9916_CR7","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","volume":"72","author":"MM Bradford","year":"1976","unstructured":"Bradford MM (1976) Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein\u2013dye binding. Anal Biochem 72:248\u2013254","journal-title":"Anal Biochem"},{"key":"9916_CR8","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1007\/s11120-011-9667-8","volume":"108","author":"AE Carmo-Silva","year":"2011","unstructured":"Carmo-Silva AE, Salvucci ME (2011) The activity of Rubisco\u2019s molecular chaperone Rubisco activase in leaf extracts. Photosynth Res 108:143\u2013155","journal-title":"Photosynth Res"},{"key":"9916_CR9","doi-asserted-by":"crossref","first-page":"4696","DOI":"10.1073\/pnas.85.13.4696","volume":"85","author":"ZX Chen","year":"1988","unstructured":"Chen ZX, Chastain CJ, Al-Abed SR, Chollet R, Spreitzer RJ (1988) Reduced CO2\/O2 specificity of ribulose-bisphosphate carboxylase oxygenase in a temperature-sensitive chloroplast mutant of Chlamydomonas. Proc Natl Acad Sci USA 85:4696\u20134699","journal-title":"Proc Natl Acad Sci USA"},{"key":"9916_CR10","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1104\/pp.101.4.1189","volume":"101","author":"ZX Chen","year":"1993","unstructured":"Chen ZX, Hong S, Spreitzer RJ (1993) Thermal instability of ribulose-1,5-bisphosphate carboxylase\/oxygenase from a temperature-conditional chloroplast mutant of Chlamydomonas reinhardtii. Plant Physiol 101:1189\u20131194","journal-title":"Plant Physiol"},{"key":"9916_CR11","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1016\/S0076-6879(80)69042-9","volume":"69","author":"NH Chua","year":"1980","unstructured":"Chua NH (1980) Electrophoretic analysis of chloroplast proteins. Methods Enzymol 69:434\u2013446","journal-title":"Methods Enzymol"},{"key":"9916_CR12","doi-asserted-by":"crossref","first-page":"14206","DOI":"10.1073\/pnas.260503997","volume":"97","author":"YC Du","year":"2000","unstructured":"Du YC, Hong S, Spreitzer RJ (2000) RbcS suppressor mutations improve the thermal stability and CO2\/O2 specificity of rbcL-mutant ribulose-1,5-bisphosphate carboxylase\/oxygenase. Proc Natl Acad Sci USA 97:14206\u201314211","journal-title":"Proc Natl Acad Sci USA"},{"key":"9916_CR13","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1006\/jmbi.2000.3724","volume":"298","author":"AP Duff","year":"2000","unstructured":"Duff AP, Andrews TJ, Curmi PMG (2000) The transition between the open and closed states of Rubisco is triggered by the inter-phosphate distance of the bound bisphosphate. J Mol Biol 298:903\u2013916","journal-title":"J Mol Biol"},{"key":"9916_CR14","doi-asserted-by":"crossref","first-page":"5745","DOI":"10.1021\/bi052588y","volume":"45","author":"MG Esquivel","year":"2006","unstructured":"Esquivel MG, Pinto TS, Mar\u00edn-Navarro J, Moreno J (2006) Substitution of tyrosine residues at the aromatic cluster around the \u03b2A-\u03b2B loop of rubisco small subunit affects the structural stability of the enzyme and the in vivo degradation under stress conditions. Biochemistry 45:5745\u20135753","journal-title":"Biochemistry"},{"key":"9916_CR15","doi-asserted-by":"crossref","first-page":"30105","DOI":"10.1074\/jbc.M109.044081","volume":"284","author":"T Genkov","year":"2009","unstructured":"Genkov T, Spreitzer RJ (2009) Highly conserved small subunit residues influence Rubisco large-subunit catalysis. J Biol Chem 284:30105\u201330112","journal-title":"J Biol Chem"},{"key":"9916_CR16","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.abb.2006.04.012","volume":"451","author":"T Genkov","year":"2006","unstructured":"Genkov T, Du YC, Spreitzer RJ (2006) Small-subunit cysteine-65 substitutions can suppress or induce alterations in the large-subunit catalytic efficiency and holoenzyme thermal stability of ribulose-1,5-bisphosphate carboxylase\/oxygenase. Arch Biochem Biophys 451:167\u2013174","journal-title":"Arch Biochem Biophys"},{"key":"9916_CR17","doi-asserted-by":"crossref","first-page":"19833","DOI":"10.1074\/jbc.M110.124230","volume":"285","author":"T Genkov","year":"2010","unstructured":"Genkov T, Meyer M, Griffiths H, Spreitzer RJ (2010) Functional hybrid Rubisco enzymes with plant small subunits and algal large subunits: engineered rbcS cDNA for expression in Chlamydomonas. J Biol Chem 285:19833\u201319841","journal-title":"J Biol Chem"},{"key":"9916_CR18","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1006\/jmbi.1999.2701","volume":"288","author":"S Hansen","year":"1999","unstructured":"Hansen S, Vollan VB, Hough E, Andersen K (1999) The crystal structure of Rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded \u03b2-barrel formed by \u03b2-strands from four subunits. J Mol Biol 288:609\u2013621","journal-title":"J Mol Biol"},{"key":"9916_CR19","doi-asserted-by":"crossref","first-page":"11114","DOI":"10.1074\/jbc.272.17.11114","volume":"272","author":"S Hong","year":"1997","unstructured":"Hong S, Spreitzer RJ (1997) Complementing substitutions at the bottom of the barrel influence catalysis and stability of ribulose-bisphosphate carboxylase\/oxygenase. J Biol Chem 272:11114\u201311117","journal-title":"J Biol Chem"},{"key":"9916_CR20","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1093\/oxfordjournals.pcp.a029191","volume":"38","author":"H Ishida","year":"1997","unstructured":"Ishida H, Nishimori Y, Sugisawa M, Makino A, Mae T (1997) The large subunit of ribulose-1,5-bisphosphate carboxylase\/oxygenase is fragmented into 37-kDa and 16-kDa polypeptides by active oxygen in the lysates of chloroplasts from primary leaves of wheat. Plant Cell Physiol 38:471\u2013479","journal-title":"Plant Cell Physiol"},{"key":"9916_CR21","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1104\/pp.67.2.237","volume":"67","author":"DB Jordan","year":"1981","unstructured":"Jordan DB, Ogren WL (1981) A sensitive assay procedure for simultaneous determination of ribulose-1,5-bisphosphate carboxylase and oxygenase activities. Plant Physiol 67:237\u2013245","journal-title":"Plant Physiol"},{"key":"9916_CR22","doi-asserted-by":"crossref","first-page":"9851","DOI":"10.1021\/bi050537v","volume":"44","author":"S Karkehabadi","year":"2005","unstructured":"Karkehabadi S, Peddi SR, Anwaruzzaman M, Taylor TC, Cederlund A, Genkov T, Andersson I, Spreitzer RJ (2005a) Chimeric small subunits influence catalysis without causing global conformational changes in the crystal structure of ribulose-1,5-bisphosphate carboxylase\/oxygenase. Biochemistry 44:9851\u20139861","journal-title":"Biochemistry"},{"key":"9916_CR23","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1021\/bi047928e","volume":"44","author":"S Karkehabadi","year":"2005","unstructured":"Karkehabadi S, Taylor TC, Spreitzer RJ, Andersson I (2005b) Altered intersubunit interactions in crystal structures of catalytically compromised ribulose-1,5-bisphosphate carboxylase\/oxygenase. Biochemistry 44:113\u2013120","journal-title":"Biochemistry"},{"key":"9916_CR24","doi-asserted-by":"crossref","first-page":"13689","DOI":"10.1073\/pnas.93.24.13689","volume":"93","author":"I Khrebtukova","year":"1996","unstructured":"Khrebtukova I, Spreitzer RJ (1996) Elimination of the Chlamydomonas gene family that encodes the small subunit of ribulose-1,5-bisphosphate carboxylase\/oxygenase. Proc Natl Acad Sci USA 93:13689\u201313693","journal-title":"Proc Natl Acad Sci USA"},{"key":"9916_CR25","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1042\/bj1750909","volume":"175","author":"GD Kuehn","year":"1978","unstructured":"Kuehn GD, Hsu TC (1978) Preparative-scale enzymic synthesis of D-[14C]ribulose-1,5-bisphosphate. Biochem J 175:909\u2013912","journal-title":"Biochem J"},{"key":"9916_CR26","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1104\/pp.54.5.678","volume":"54","author":"WA Laing","year":"1974","unstructured":"Laing WA, Ogren WL, Hageman RH (1974) Regulation of soybean net photosynthetic CO2 fixation by the interaction of CO2, O2 and ribulose 1,5-diphosphate carboxylase. Plant Physiol 54:678\u2013685","journal-title":"Plant Physiol"},{"key":"9916_CR27","doi-asserted-by":"crossref","first-page":"17033","DOI":"10.1074\/jbc.272.27.17033","volume":"272","author":"EM Larson","year":"1997","unstructured":"Larson EM, O\u2019Brien CM, Zhu G, Spreitzer RJ, Portis AR (1997) Specificity for activase is changed by a Pro-89 to Arg substitution in the large subunit of ribulose-1,5-bisphosphate carboxylase\/oxygenase. J Biol Chem 272:17033\u201317037","journal-title":"J Biol Chem"},{"key":"9916_CR28","doi-asserted-by":"crossref","first-page":"29323","DOI":"10.1074\/jbc.M703896200","volume":"282","author":"BM Long","year":"2007","unstructured":"Long BM, Badger MR, Whitney SM, Price GD (2007) Analysis of carboxysomes from Synechococcus PCC7942 reveals multiple Rubisco complexes with carboxysomal proteins CcmM and CcaA. J Biol Chem 282:29323\u201329335","journal-title":"J Biol Chem"},{"key":"9916_CR29","doi-asserted-by":"crossref","first-page":"19474","DOI":"10.1073\/pnas.1210993109","volume":"109","author":"MT Meyer","year":"2012","unstructured":"Meyer MT, Genkov T, Skepper JN, Jouhet U, Mitchell MC, Spreitzer RJ, Griffiths H (2012) Rubisco small-subunit \u03b1-helices control pyrenoid formation in Chlamydomonas. Proc Natl Acad Sci USA 109:19474\u201319479","journal-title":"Proc Natl Acad Sci USA"},{"key":"9916_CR30","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1038\/nature10568","volume":"479","author":"O Mueller-Cajar","year":"2011","unstructured":"Mueller-Cajar O, Stotz M, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M (2011) Structure and function of the AAA\u00a0+\u00a0protein CbbX, a red-type Rubisco activase. Nature 479:194\u2013199","journal-title":"Nature"},{"key":"9916_CR31","doi-asserted-by":"crossref","first-page":"25876","DOI":"10.1016\/S0021-9258(19)74469-X","volume":"268","author":"J Newman","year":"1993","unstructured":"Newman J, Gutteridge S (1993) The X-ray structure of Synechococcus ribulose-bisphosphate carboxylase\/oxygenase activated quaternary complex at 2.2-\u00c5 resolution. J Biol Chem 268:25876\u201365886","journal-title":"J Biol Chem"},{"key":"9916_CR32","doi-asserted-by":"crossref","first-page":"26241","DOI":"10.1074\/jbc.M004580200","volume":"275","author":"CM Ott","year":"2000","unstructured":"Ott CM, Smith BD, Portis AR Jr, Spreitzer RJ (2000) Activase region on chloroplast ribulose-1,5-bisphosphate carboxylase\/oxygenase. Nonconservative substitution in the large subunit alters species specificity of protein interaction. J Biol Chem 275:26241\u201326244","journal-title":"J Biol Chem"},{"key":"9916_CR33","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1080\/08924562.1996.11000299","volume":"9","author":"C Papworth","year":"1996","unstructured":"Papworth C, Bauer JC, Braman J, Wright DA (1996) Site-directed mutagenesis in one day with greater than 80% efficiency. Strategies 9:3\u20134","journal-title":"Strategies"},{"key":"9916_CR34","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.1093\/jxb\/erm240","volume":"59","author":"AR Portis Jr","year":"2008","unstructured":"Portis AR Jr, Li C, Wang D, Salvucci ME (2008) Regulation of Rubisco activase and its interaction with Rubisco. J Exp Bot 59:1597\u20131604","journal-title":"J Exp Bot"},{"key":"9916_CR35","doi-asserted-by":"crossref","first-page":"14240","DOI":"10.1074\/jbc.M313215200","volume":"279","author":"S Satagopan","year":"2004","unstructured":"Satagopan S, Spreitzer RJ (2004) Substitutions at the Asp-473 latch residue of Chlamydomonas ribulosebisphosphate carboxylase\/oxygenase cause decreases in carboxylation efficiency and CO2\/O2 specificity. J Biol Chem 279:14240\u201314244","journal-title":"J Biol Chem"},{"key":"9916_CR36","doi-asserted-by":"crossref","first-page":"9968","DOI":"10.1073\/pnas.90.21.9968","volume":"90","author":"HA Schreuder","year":"1993","unstructured":"Schreuder HA, Knight S, Curmi PM, Andersson I, Cascio D, Branden CI, Eisenberg D (1993) Formation of the active site of ribulose-1,5-bisphosphate carboxylase\/oxygenase by a disorder-order transition from the unactivated to the activated form. Proc Natl Acad Sci USA 90:9968\u20139972","journal-title":"Proc Natl Acad Sci USA"},{"key":"9916_CR37","doi-asserted-by":"crossref","first-page":"1821","DOI":"10.1093\/genetics\/148.4.1821","volume":"148","author":"K Shimogawara","year":"1998","unstructured":"Shimogawara K, Fujiwara S, Grossman A, Usuda H (1998) High-efficiency transformation of Chlamydomonas reinhardtii by electroporation. Genetics 148:1821\u20131828","journal-title":"Genetics"},{"key":"9916_CR38","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/S0003-9861(03)00171-1","volume":"414","author":"RJ Spreitzer","year":"2003","unstructured":"Spreitzer RJ (2003) Role of the small subunit in ribulose-1,5-bisphosphate carboxylase\/oxygenase. Arch Biochem Biophys 414:141\u2013149","journal-title":"Arch Biochem Biophys"},{"key":"9916_CR39","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1007\/BF00393924","volume":"11","author":"RJ Spreitzer","year":"1987","unstructured":"Spreitzer RJ, Chastain CJ (1987) Heteroplasmic suppression of an amber mutation in the Chlamydomonas chloroplast gene that encodes the large subunit of ribulosebisphosphate carboxylase\/oxygenase. Curr Genet 11:611\u2013616","journal-title":"Curr Genet"},{"key":"9916_CR40","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1104\/pp.67.3.565","volume":"67","author":"RJ Spreitzer","year":"1981","unstructured":"Spreitzer RJ, Mets L (1981) Photosynthesis-deficient mutants of Chlamydomonas reinhardtii with associated light-sensitive phenotypes. Plant Physiol 67:565\u2013569","journal-title":"Plant Physiol"},{"key":"9916_CR41","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1146\/annurev.arplant.53.100301.135233","volume":"53","author":"RJ Spreitzer","year":"2002","unstructured":"Spreitzer RJ, Salvucci ME (2002) Rubisco: structure, regulatory interactions, and possibilities for a better enzyme. Annu Rev Plant Biol 53:449\u2013475","journal-title":"Annu Rev Plant Biol"},{"key":"9916_CR42","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/0014-5793(82)81255-6","volume":"148","author":"RJ Spreitzer","year":"1982","unstructured":"Spreitzer RJ, Jordan DB, Ogren WL (1982) Biochemical and genetic analysis of an RuBP carboxylase\/oxygenase-deficient mutant and revertants of Chlamydomonas reinhardtii. FEBS Lett 148:117\u2013121","journal-title":"FEBS Lett"},{"key":"9916_CR43","doi-asserted-by":"crossref","first-page":"5615","DOI":"10.1021\/bi002943e","volume":"40","author":"RJ Spreitzer","year":"2001","unstructured":"Spreitzer RJ, Esquivel MG, Du YC, McLaughlin PD (2001) Alanine-scanning mutagenesis of the small-subunit \u03b2A-\u03b2B loop of chloroplast ribulose-1,5-bisphosphate carboxylase\/oxygenase: substitution at Arg-71 affects thermal stability and CO2\/O2 specificity. Biochemistry 40:5615\u20135621","journal-title":"Biochemistry"},{"key":"9916_CR44","doi-asserted-by":"crossref","first-page":"17225","DOI":"10.1073\/pnas.0508042102","volume":"102","author":"RJ Spreitzer","year":"2005","unstructured":"Spreitzer RJ, Peddi SR, Satagopan S (2005) Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco. Proc Natl Acad Sci USA 102:17225\u201317230","journal-title":"Proc Natl Acad Sci USA"},{"key":"9916_CR45","doi-asserted-by":"crossref","first-page":"15655","DOI":"10.1074\/jbc.274.22.15655","volume":"274","author":"H Sugawara","year":"1999","unstructured":"Sugawara H, Yamamoto H, Shibata N, Inoue T, Okada S, Miyake C, Yokota A, Yasushi K (1999) Crystal structure of carboxylase reaction-oriented ribulose-1,5-bisphosphate carboxylase\/oxygenase from a thermophilic red alga, Galdieria partita. J Biol Chem 274:15655\u201315661","journal-title":"J Biol Chem"},{"key":"9916_CR46","doi-asserted-by":"crossref","first-page":"48159","DOI":"10.1074\/jbc.M107765200","volume":"276","author":"TC Taylor","year":"2001","unstructured":"Taylor TC, Backlund A, Bjorhall K, Spreitzer RJ, Andersson I (2001) First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii. J Biol Chem 276:48159\u201348164","journal-title":"J Biol Chem"},{"key":"9916_CR47","doi-asserted-by":"crossref","first-page":"5109","DOI":"10.1021\/bi00183a014","volume":"33","author":"G Thow","year":"1994","unstructured":"Thow G, Zhu G, Spreitzer RJ (1994) Complementing substitutions within loop regions 2 and 3 of the \u03b1\/\u03b2-barrel active site influence the CO2\/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase\/oxygenase. Biochemistry 33:5109\u20135114","journal-title":"Biochemistry"},{"key":"9916_CR48","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1016\/j.jmb.2011.06.052","volume":"411","author":"M Lun van","year":"2011","unstructured":"van Lun M, van der Spoel D, Andersson I (2011) Subunit interface dynamics in hexadecameric Rubisco. J Mol Biol 411:1083\u20131098","journal-title":"J Mol Biol"},{"key":"9916_CR49","author":"RM Wachter","year":"2013","unstructured":"Wachter RM, Salvucci ME, Carmo-Silva AE, Barta C, Genkov T, Spreitzer RJ (2013) Activation of interspecies-hybrid Rubisco enzymes to assess different models for the Rubisco\u2013Rubisco activase interaction. Photosynth Res. doi: 10.1007\/s11120-013-9827-0","journal-title":"Photosynth Res"}],"container-title":["Photosynthesis Research"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11120-013-9916-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s11120-013-9916-0\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11120-013-9916-0","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,5]],"date-time":"2022-03-05T17:46:47Z","timestamp":1646502407000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s11120-013-9916-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,9,7]]},"references-count":49,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2013,12]]}},"alternative-id":["9916"],"URL":"https:\/\/doi.org\/10.1007\/s11120-013-9916-0","relation":{},"ISSN":["0166-8595","1573-5079"],"issn-type":[{"value":"0166-8595","type":"print"},{"value":"1573-5079","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,9,7]]}}}