Oxygen uncouples light absorption by the chlorosome antenna and photosynthetic electron transfer in the green sulfur bacterium Chlorobium tepidum

N-U Frigaard; K Matsuura

doi:10.1016/S0005-2728(99)00060-2

Oxygen uncouples light absorption by the chlorosome antenna and photosynthetic electron transfer in the green sulfur bacterium Chlorobium tepidum

N-U Frigaard, K Matsuura

Bioinformatik og RNA Biologi

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

24 Citationer (Scopus)

Abstract

Udgivelsesdato: 30 June 1999

Originalsprog	Engelsk
Tidsskrift	BBA General Subjects
Vol/bind	1412
Udgave nummer	2
Sider (fra-til)	108-117
Antal sider	10
ISSN	0304-4165
DOI	https://doi.org/10.1016/S0005-2728(99)00060-2
Status	Udgivet - 1999

Bibliografisk note

Author Keywords: Green bacterium; Chlorosome; Excitation energy transfer; Fluorescence quenching; Cytochrome c photooxidation; Reactive oxygen species

Adgang til dokumentet

10.1016/S0005-2728(99)00060-2

Citationsformater

@article{482e7a30962711de8bc9000ea68e967b,

title = "Oxygen uncouples light absorption by the chlorosome antenna and photosynthetic electron transfer in the green sulfur bacterium Chlorobium tepidum",

abstract = "In photosynthetic green sulfur bacteria excitation energy is transferred from large bacteriochlorophyll (BChl) c chlorosome antennas via small BChl a antennas to the reaction centers which then transfer electrons from cytochrome c to low-potential iron-sulfur proteins. Under oxidizing conditions a reversible mechanism is activated in the chlorosomes which quenches excited BChl c. We used flash-induced cytochrome c oxidation to investigate the effect of this quenching on photosynthetic electron transfer in whole cells of Chlorobium tepidum. The extent of cytochrome c photooxidation under aerobic conditions decreased to approx. 3% of that under anaerobic conditions when BChl c was excited under light-limiting conditions. Photooxidation obtained by excitation of BChl a was similar under aerobic and anaerobic conditions. We interpret this drastic decrease in energy transfer from BChl c to the reaction center as a consequence of the quenching mechanism which is activated by O2. This reversible uncoupling of the chlorosome antenna might prevent formation of toxic reactive oxygen species from photosynthetically produced reductants under aerobic conditions. The green filamentous bacterium Chloroflexus aurantiacus also contains chlorosomes but energy transfer from the BChl c and BChl a antennas to the reaction center in this species was not affected by O2.",

author = "N-U Frigaard and K Matsuura",

note = "Author Keywords: Green bacterium; Chlorosome; Excitation energy transfer; Fluorescence quenching; Cytochrome c photooxidation; Reactive oxygen species",

year = "1999",

doi = "10.1016/S0005-2728(99)00060-2",

language = "English",

volume = "1412",

pages = "108--117",

journal = "B B A - General Subjects",

issn = "0304-4165",

publisher = "Elsevier",

number = "2",

}

TY - JOUR

T1 - Oxygen uncouples light absorption by the chlorosome antenna and photosynthetic electron transfer in the green sulfur bacterium Chlorobium tepidum

AU - Frigaard, N-U

AU - Matsuura, K

N1 - Author Keywords: Green bacterium; Chlorosome; Excitation energy transfer; Fluorescence quenching; Cytochrome c photooxidation; Reactive oxygen species

PY - 1999

Y1 - 1999

N2 - In photosynthetic green sulfur bacteria excitation energy is transferred from large bacteriochlorophyll (BChl) c chlorosome antennas via small BChl a antennas to the reaction centers which then transfer electrons from cytochrome c to low-potential iron-sulfur proteins. Under oxidizing conditions a reversible mechanism is activated in the chlorosomes which quenches excited BChl c. We used flash-induced cytochrome c oxidation to investigate the effect of this quenching on photosynthetic electron transfer in whole cells of Chlorobium tepidum. The extent of cytochrome c photooxidation under aerobic conditions decreased to approx. 3% of that under anaerobic conditions when BChl c was excited under light-limiting conditions. Photooxidation obtained by excitation of BChl a was similar under aerobic and anaerobic conditions. We interpret this drastic decrease in energy transfer from BChl c to the reaction center as a consequence of the quenching mechanism which is activated by O2. This reversible uncoupling of the chlorosome antenna might prevent formation of toxic reactive oxygen species from photosynthetically produced reductants under aerobic conditions. The green filamentous bacterium Chloroflexus aurantiacus also contains chlorosomes but energy transfer from the BChl c and BChl a antennas to the reaction center in this species was not affected by O2.

AB - In photosynthetic green sulfur bacteria excitation energy is transferred from large bacteriochlorophyll (BChl) c chlorosome antennas via small BChl a antennas to the reaction centers which then transfer electrons from cytochrome c to low-potential iron-sulfur proteins. Under oxidizing conditions a reversible mechanism is activated in the chlorosomes which quenches excited BChl c. We used flash-induced cytochrome c oxidation to investigate the effect of this quenching on photosynthetic electron transfer in whole cells of Chlorobium tepidum. The extent of cytochrome c photooxidation under aerobic conditions decreased to approx. 3% of that under anaerobic conditions when BChl c was excited under light-limiting conditions. Photooxidation obtained by excitation of BChl a was similar under aerobic and anaerobic conditions. We interpret this drastic decrease in energy transfer from BChl c to the reaction center as a consequence of the quenching mechanism which is activated by O2. This reversible uncoupling of the chlorosome antenna might prevent formation of toxic reactive oxygen species from photosynthetically produced reductants under aerobic conditions. The green filamentous bacterium Chloroflexus aurantiacus also contains chlorosomes but energy transfer from the BChl c and BChl a antennas to the reaction center in this species was not affected by O2.

U2 - 10.1016/S0005-2728(99)00060-2

DO - 10.1016/S0005-2728(99)00060-2

M3 - Journal article

C2 - 10393254

VL - 1412

SP - 108

EP - 117

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 2

ER -