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Title: Isolation and characterization of photosynthetic reaction centers from Rhodopseudomonas capsulata and Rhodopseudomonas sphaeroides

Abstract

Reaction centers were isolated by affinity chromatography on equine cytochrome C. Peripheral proteins were removed with 0.05% LDAO. Absorption and EPR spectra and bleaching assays indicate that the reaction centers retained their electron donors and acceptors in the native environment. Three reaction center polypeptides were isolated and submitted for amino-terminal sequence determination. By comparing these sequences to those deduced from DNA, it was established that the M and L subunits are post-translationally modified to remove the aminoterminal Met, whereas the H subunit is not. Inhibition of O/sub 2/ evolution in photosystem II particles from spinach by naphthoquinone derivatives show O/sub 2/ inhibition by bromomethyl and acetoxymethyl derivatives but not with hydroxymethyl derivatives. Inhibition by acetoxymethyl derivatives in irreversible and dependent on illumination suggesting that reduction of the quinone is necessary. Therefore acetoxymethyl derivatives may be useful as suicide reagents for labelling quinone binding sites. Procedures were developed to extract one or both of the quinones present in reaction centers and preserve the integrity of the co-factor binding sites. The H and M subunits were cleaned using furmic acid. Both fragments were isolated from the H subunit, while the larger fragment was isolated from the M subunit. Electrophoretic mobilities of themore » isolated fragments agrees well with the expected molecular weights. The L subunit was digested with Staphylococcus areus vs protease. The pattern obtained was consistant with the potential sites of cleavage, but it was not possible to assign cleavage sites unambiguously. 112 references, 37 figures, 2 tables.« less

Authors:
Publication Date:
Research Org.:
Lawrence Berkeley Lab., CA (USA)
OSTI Identifier:
6414236
Report Number(s):
LBL-18375
ON: DE85000623
DOE Contract Number:  
AC03-76SF00098
Resource Type:
Technical Report
Resource Relation:
Other Information: Portions are illegible in microfiche products. Thesis
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; RHODOPSEUDOMONAS; PHOTOSYNTHETIC REACTION CENTERS; AMINO ACID SEQUENCE; BIOCHEMICAL REACTION KINETICS; ELECTROPHORESIS; EXPERIMENTAL DATA; INHIBITION; OXYGEN; PHOTOCHEMICAL REACTIONS; PRODUCTION; QUINONES; VISIBLE RADIATION; AROMATICS; BACTERIA; CHEMICAL REACTIONS; DATA; ELECTROMAGNETIC RADIATION; ELEMENTS; INFORMATION; KINETICS; MICROORGANISMS; MOLECULAR STRUCTURE; NONMETALS; NUMERICAL DATA; ORGANIC COMPOUNDS; ORGANIC OXYGEN COMPOUNDS; RADIATIONS; REACTION KINETICS; 550200* - Biochemistry; 550700 - Microbiology

Citation Formats

Worland, S T. Isolation and characterization of photosynthetic reaction centers from Rhodopseudomonas capsulata and Rhodopseudomonas sphaeroides. United States: N. p., 1984. Web.
Worland, S T. Isolation and characterization of photosynthetic reaction centers from Rhodopseudomonas capsulata and Rhodopseudomonas sphaeroides. United States.
Worland, S T. 1984. "Isolation and characterization of photosynthetic reaction centers from Rhodopseudomonas capsulata and Rhodopseudomonas sphaeroides". United States.
@article{osti_6414236,
title = {Isolation and characterization of photosynthetic reaction centers from Rhodopseudomonas capsulata and Rhodopseudomonas sphaeroides},
author = {Worland, S T},
abstractNote = {Reaction centers were isolated by affinity chromatography on equine cytochrome C. Peripheral proteins were removed with 0.05% LDAO. Absorption and EPR spectra and bleaching assays indicate that the reaction centers retained their electron donors and acceptors in the native environment. Three reaction center polypeptides were isolated and submitted for amino-terminal sequence determination. By comparing these sequences to those deduced from DNA, it was established that the M and L subunits are post-translationally modified to remove the aminoterminal Met, whereas the H subunit is not. Inhibition of O/sub 2/ evolution in photosystem II particles from spinach by naphthoquinone derivatives show O/sub 2/ inhibition by bromomethyl and acetoxymethyl derivatives but not with hydroxymethyl derivatives. Inhibition by acetoxymethyl derivatives in irreversible and dependent on illumination suggesting that reduction of the quinone is necessary. Therefore acetoxymethyl derivatives may be useful as suicide reagents for labelling quinone binding sites. Procedures were developed to extract one or both of the quinones present in reaction centers and preserve the integrity of the co-factor binding sites. The H and M subunits were cleaned using furmic acid. Both fragments were isolated from the H subunit, while the larger fragment was isolated from the M subunit. Electrophoretic mobilities of the isolated fragments agrees well with the expected molecular weights. The L subunit was digested with Staphylococcus areus vs protease. The pattern obtained was consistant with the potential sites of cleavage, but it was not possible to assign cleavage sites unambiguously. 112 references, 37 figures, 2 tables.},
doi = {},
url = {https://www.osti.gov/biblio/6414236}, journal = {},
number = ,
volume = ,
place = {United States},
year = {Sat Sep 01 00:00:00 EDT 1984},
month = {Sat Sep 01 00:00:00 EDT 1984}
}

Technical Report:
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