Nuclear pea mutants deficient in chlorophyll b and the major polypeptide of the light-harvesting chlorophyll a/b protein of photosystem II View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1984-12

AUTHORS

Bjarne M. Stummann, Knud W. Henningsen

ABSTRACT

Eight chlorophyll b deficient nuclear mutants of pea (Pisum sativum L.) have been characterized by low temperature fluorescence emission spectra of their leaves and by the ultrastructure, photochemical activities and polypeptide compositions of the thylakoid membranes. The room temperature fluorescence induction kinetics of leaves and isolated thylakoids have also been recorded. In addition, the effects of Mg(2+) on the fluorescence kinetics of the membranes have been investigated. The mutants are all deficient in the major polypeptide of the light-harvesting chlorophyll a/b protein of photosystem II. The low temperature fluorescence emission spectra of aurea-5106, xantha-5371 and -5820 show little or no fluorescence around 730 nm (photosystem I fluorescence), but possess maxima at 685 and 695 nm (photosystem II fluorescence). These three mutants have low photosystem II activities, but significant photosystem I activities. The long-wavelength fluorescence maximum is reduced for three other mutants. The Mg(2+) effect on the variable component of the room temperature fluorescence (685 nm) induction kinetics is reduced in all mutants, and completely absent in aurea-5106 and xantha-5820. The thylakoid membranes of these 2 mutants are appressed pairwise in 2-disc grana of large diameter. Chlorotica-1-206A and-130A have significant long-wavelength maxima in the fluorescence spectra and show the largest Mg(2+) enhancement of the variable part of the fluorescence kinetics. These two mutants have rather normally structured chloroplast membranes, though the stroma regions are reduced. The four remaining mutants are in several respects of an intermediate type. More... »

PAGES

275-292

Journal

TITLE

Photosynthesis Research

ISSUE

4

VOLUME

5

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00034973

DOI

http://dx.doi.org/10.1007/bf00034973

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1032298112

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24458771


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