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PMID: 15178478 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Cyclic electron flow under saturating excitation of dark-adapted Arabidopsis leaves.

Biochimica et biophysica acta ·Vol. 1656 ·No. 2-3 ·2004-06-07 ·Pages 166-76

Joliot P, Béal D, Joliot A

Abstract

The rate of cyclic electron flow measured in dark-adapted leaves under aerobic conditions submitted to a saturating illumination has been performed by the analysis of the transmembrane potential changes induced by a light to dark transfer. Using a new highly sensitive spectrophotometric technique, a rate of the cyclic flow of approximately 130 s(-1) has been measured in the presence or absence of 3-(3,4-dichloro-phenyl)-1,1-dimethylurea (DCMU). This value is approximately 1.5 times larger than that previously reported [Proc. Natl. Acad. Sci. U. S. A. 99 (2001) 10209]. We have characterized in the presence or absence of DCMU charge recombination process (t(1/2) approximately 60 micros) that involves P(700)(+) and very likely the reduced form of the iron sulfur acceptor F(X). This led to conclude that, under saturating illumination, the PSI centers involved in the cyclic pathway have most of the iron sulfur acceptors F(A) and F(B) reduced. In the proposed mechanism, electrons are transferred from a ferredoxin bound to a site localized on the stromal side of the cytochrome b(6)f complex to the Q(i) site. Two possible models of the organization of the membrane complexes are discussed, in which the cyclic and linear electron transfer chains are isolated one from the other.

MeSH Terms
Adaptation, Physiological Aerobiosis Arabidopsis/anatomy & histology,physiology Cytochrome b Group/metabolism Darkness Diuron/pharmacology Electron Transport/radiation effects Ferredoxins/metabolism Iron/metabolism Kinetics Light Membrane Potentials/drug effects,radiation effects Models, Biological Photosystem I Protein Complex/drug effects,metabolism Photosystem II Protein Complex/drug effects,metabolism Plant Leaves/metabolism Plant Proteins/metabolism Sensitivity and Specificity Spectrophotometry/instrumentation,methods Sulfur/metabolism
Chemicals
Cytochrome b Group Ferredoxins Photosystem I Protein Complex Photosystem II Protein Complex Plant Proteins Sulfur Diuron Iron
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Joliot Pierre
Institut de Biologie Physico-Chimique, CNRS UPR 1261, 13, rue Pierre-et-Marie Curie, 75005 Paris, France. [email protected]
Béal Daniel
Joliot Anne
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
2004-06-07
Pages
166-76
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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