Purification of a Photosystem II reaction center from a thermophilic cyanobacterium using immobilized metal affinity chromatography View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-03

AUTHORS

Eva Šetlíková, Stephan Ritter, Rainer Hienerwadel, Jiří Kopecký, Josef Komenda, Wolfram Welte, Ivan Šetlík

ABSTRACT

Oxygen-evolving PS II particles from the thermophilic cyanobacterium Synechococcus elongatus are partially purified by centrifugation on a sucrose gradient and are bound to a Chelating Sepharose column loaded with Cu2+ ions. Bound particles are then transformed into PS II RC complexes by two washing steps. First, washing with a phosphate buffer (pH=6.5) containing 0.02% of SB 12 removes the rest of phycobilins and leaves pure PS II core particles on the column. Second, washing with a phosphate buffer (pH=6.2) containing 0.2 M LiClO4 and 0.05% of DM removes CP 47 and CP 43 and leaves bare PS II RC complexes on the column. These are then eluted with a phosphate buffer containing 1% of dodecylmaltoside (DM). The molar ratio of pigments in the eluate changes with the progress of elution but around the middle of the elution period a nearly stable ratio is maintained of Chl a: Pheo a: Car: Cyt b 559 equal to 2.9: 1: 0.9: 0.8. In these fractions the photochemical separation of charges could be demonstrated by accumulation of reduced pheophytin (ΔA of 430–440 nm) and by the flash induced formation of P680+ (ΔA at 820 nm). The relatively slow relaxation kinetics of the latter signal (t1/2 ≈ 1 ms) may suggest that in a substantial fraction of the RCs QA remains bound to the complex. More... »

PAGES

201-211

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00029933

DOI

http://dx.doi.org/10.1007/bf00029933

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1019956802

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24306843


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