A peroxidase homologue and novel plastocyanin located by proteomics to the Arabidopsis chloroplast thylakoid lumen. Kieselbach, T., Bystedt, M., Hynds, P., Robinson, C., & Schröder, W. P. FEBS Letters, 480(2-3):271–276, 2000. _eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793%2800%2901890-1
A peroxidase homologue and novel plastocyanin located by proteomics to the Arabidopsis chloroplast thylakoid lumen [link]Paper  doi  abstract   bibtex   
A study by two-dimensional electrophoresis showed that the soluble, lumenal fraction of Arabidopsis thaliana thylakoids can be resolved into 300 protein spots. After subtraction of low-intensity spots and accounting for low-level stromal contamination, the number of more abundant, lumenal proteins was estimated to be between 30 and 60. Two of these proteins have been identified: a novel plastocyanin that also was the predominant component of the total plastocyanin pool, and a putative ascorbate peroxidase. Import studies showed that these proteins are routed to the thylakoid lumen by the Sec- and delta pH-dependent translocation pathways, respectively. In addition, novel isoforms of PsbO and PsbQ were identified.
@article{kieselbach_peroxidase_2000,
	title = {A peroxidase homologue and novel plastocyanin located by proteomics to the {Arabidopsis} chloroplast thylakoid lumen},
	volume = {480},
	copyright = {FEBS Letters 480 (2000) 1873-3468 © 2015 Federation of European Biochemical Societies},
	issn = {1873-3468},
	url = {https://onlinelibrary.wiley.com/doi/abs/10.1016/S0014-5793%2800%2901890-1},
	doi = {10.1016/S0014-5793(00)01890-1},
	abstract = {A study by two-dimensional electrophoresis showed that the soluble, lumenal fraction of Arabidopsis thaliana thylakoids can be resolved into 300 protein spots. After subtraction of low-intensity spots and accounting for low-level stromal contamination, the number of more abundant, lumenal proteins was estimated to be between 30 and 60. Two of these proteins have been identified: a novel plastocyanin that also was the predominant component of the total plastocyanin pool, and a putative ascorbate peroxidase. Import studies showed that these proteins are routed to the thylakoid lumen by the Sec- and delta pH-dependent translocation pathways, respectively. In addition, novel isoforms of PsbO and PsbQ were identified.},
	language = {en},
	number = {2-3},
	urldate = {2021-11-08},
	journal = {FEBS Letters},
	author = {Kieselbach, Thomas and Bystedt, Maria and Hynds, Peter and Robinson, Colin and Schröder, Wolfgang P.},
	year = {2000},
	note = {\_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793\%2800\%2901890-1},
	keywords = {AC, MALDI-TOF-MS, Oxygen evolution, Photosystem II, Protein import, SDS–PAGE, Twin-arginine translocase, accession number, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, pH translocation pathway, sodium dodecyl sulfate–polyacrylamide gel electrophoresis},
	pages = {271--276},
}

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