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פותח על ידי קלירמאש פתרונות בע"מ -
2,3-Dimercaptopropan-1-ol (BAL). An aerobic electron-transport inhibitor, but an anaerobic photosynthetic electron donor
Year:
1984
Source of publication :
BBA - Bioenergetics
Authors :
שחק, יוספה
;
.
Volume :
766
Co-Authors:
Belkin, S., Division of Microbial and Molecular Ecology, The Institute of Life Sciences, The Hebrew University, Jerusalem, Israel
Siderer, Y., Division of Microbial and Molecular Ecology, The Institute of Life Sciences, The Hebrew University, Jerusalem, Israel
Shahak, Y., Biochemistry Department, Weizmann Institute of Science, Rehovot, 76100, Israel
Arieli, B., Division of Microbial and Molecular Ecology, The Institute of Life Sciences, The Hebrew University, Jerusalem, Israel
Padan, E., Department of Biological Chemistry, The Institute of Life Sciences, The Hebrew University, Jerusalem, Israel
Facilitators :
From page:
563
To page:
569
(
Total pages:
7
)
Abstract:
The effect of 2,3-dimercaptopropan-1-ol (BAL) on photosynthetic electron transport was studied in Oscillatoria limnetica cells as well as in spinach chloroplasts. Preincubation of the cyanobacterial cells with BAL under aerobic conditions caused inhibition of the sulfide-dependent H2 evolution. The inhibited site was bypassed by N,N,N′,N′-tetramethyl-p-phenylene diamine. Similarly, NADP photoreduction by spinach chloroplasts was inhibited by BAL pretreatment and restored by the addition of reduced 2,6-dichlorophenol-indophenol. These results accord previous data demonstrating damage of mitochondrial Rieske iron-sulfur protein after BAL treatment (Slater, E.C. and De Vries, S. (1980) Nature 288, 717-718). However, in chloroplasts there was no change in the Rieske center ESR spectrum after BAL treatment. When added anaerobically, BAL served as an electron donor for light-dependent, H2 evolution in cyanobacteria or for NADP reduction in spinach chloroplasts. These reactions were insensitive to 3-(3′,4′-dichlorophenyl)-1,1dimethylurea (DCMU), but sensitive to 2,5-dibromothymoquinone or to aerobic pretreatment with BAL. The Rieske protein ESR signal of chloroplasts (g = 1.89) which disappeared upon illumination in the presence of DCMU and methyl viologen, was restored by BAL. It is suggested that as opposed to its aerobic inhibitory effect, BAL donates electrons to the Rieske protein under anaerobic conditions. © 1984.
Note:
Related Files :
2,3-Dimercaptopropan-1-ol
(Spinach chloroplast)
BAL
electron transport
ESR
photosynthesis
Rieske iron-sulfur protein
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/0005-2728(84)90115-4
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
20177
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:34
Scientific Publication
2,3-Dimercaptopropan-1-ol (BAL). An aerobic electron-transport inhibitor, but an anaerobic photosynthetic electron donor
766
Belkin, S., Division of Microbial and Molecular Ecology, The Institute of Life Sciences, The Hebrew University, Jerusalem, Israel
Siderer, Y., Division of Microbial and Molecular Ecology, The Institute of Life Sciences, The Hebrew University, Jerusalem, Israel
Shahak, Y., Biochemistry Department, Weizmann Institute of Science, Rehovot, 76100, Israel
Arieli, B., Division of Microbial and Molecular Ecology, The Institute of Life Sciences, The Hebrew University, Jerusalem, Israel
Padan, E., Department of Biological Chemistry, The Institute of Life Sciences, The Hebrew University, Jerusalem, Israel
2,3-Dimercaptopropan-1-ol (BAL). An aerobic electron-transport inhibitor, but an anaerobic photosynthetic electron donor
The effect of 2,3-dimercaptopropan-1-ol (BAL) on photosynthetic electron transport was studied in Oscillatoria limnetica cells as well as in spinach chloroplasts. Preincubation of the cyanobacterial cells with BAL under aerobic conditions caused inhibition of the sulfide-dependent H2 evolution. The inhibited site was bypassed by N,N,N′,N′-tetramethyl-p-phenylene diamine. Similarly, NADP photoreduction by spinach chloroplasts was inhibited by BAL pretreatment and restored by the addition of reduced 2,6-dichlorophenol-indophenol. These results accord previous data demonstrating damage of mitochondrial Rieske iron-sulfur protein after BAL treatment (Slater, E.C. and De Vries, S. (1980) Nature 288, 717-718). However, in chloroplasts there was no change in the Rieske center ESR spectrum after BAL treatment. When added anaerobically, BAL served as an electron donor for light-dependent, H2 evolution in cyanobacteria or for NADP reduction in spinach chloroplasts. These reactions were insensitive to 3-(3′,4′-dichlorophenyl)-1,1dimethylurea (DCMU), but sensitive to 2,5-dibromothymoquinone or to aerobic pretreatment with BAL. The Rieske protein ESR signal of chloroplasts (g = 1.89) which disappeared upon illumination in the presence of DCMU and methyl viologen, was restored by BAL. It is suggested that as opposed to its aerobic inhibitory effect, BAL donates electrons to the Rieske protein under anaerobic conditions. © 1984.
Scientific Publication
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