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Title: Action of heavy metals on hill activity and O/sub 2/ evolution in Anacystis nidulans

Abstract

Addition of 5 micromolar Cu/sup 2 +/, Cd/sup 2 +/, and Zn/sup 2 +/ was inhibitory to 10 micromolar H/sub 2/O/sub 2/-supported Hill activity (dichlorophenolindophenol reduction) and O/sub 2/ evolution in membrane preparation from Anacystis nidulans. The reversal of Cd/sup 2 +/ and Zn/sup 2 +/ inhibition, in contrast to Cu/sup 2 +/, by exogenously added catalase suggested that the former cations were inhibitory to H/sub 2/O/sub 2/ degradation. Ascorbic acid (20 micromolar) supported 27% of the Hill activity which was insensitive to DCMU (10 micromolar) and the remaining activity, attributable to the DCMU sensitive process, was sensitive to inhibition by Cu/sup 2 +/ only. It is suggestive that the action site of Cd/sup 2 +/ and Zn/sup 2 +/ is located between the electron donation sites of H/sub 2/O/sub 2/ and ascorbic acid, while that of Cu/sup 2 +/ is located beyond it. Electron donation by reduced glutathione was insensitive to DCMU and Cu/sup 2 +/, indicating that the action site of Cu/sup 2 +/ is prior to its electron donation site. Further, the phenanthroline (10 micromolar) reversal of Cu/sup 2 +/ inhibition of Hill activity suggested a tentative action site of Cu/sup 2 +/ at the level ofmore » cytochrome.« less

Authors:
;
Publication Date:
Research Org.:
Banaras Hindu Univ., Varanasi, India
OSTI Identifier:
6609676
Resource Type:
Journal Article
Journal Name:
Plant Physiol.; (United States)
Additional Journal Information:
Journal Volume: 83:1
Country of Publication:
United States
Language:
English
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; CADMIUM COMPOUNDS; TOXICITY; COPPER COMPOUNDS; CYANOBACTERIA; SENSITIVITY; ZINC COMPOUNDS; CATIONS; HYDROGEN PEROXIDE; INHIBITION; OXYGEN; CHARGED PARTICLES; ELEMENTS; HYDROGEN COMPOUNDS; IONS; MICROORGANISMS; NONMETALS; OXYGEN COMPOUNDS; PEROXIDES; TRANSITION ELEMENT COMPOUNDS; 560300* - Chemicals Metabolism & Toxicology

Citation Formats

Singh, D P, and Singh, S P. Action of heavy metals on hill activity and O/sub 2/ evolution in Anacystis nidulans. United States: N. p., 1987. Web.
Singh, D P, & Singh, S P. Action of heavy metals on hill activity and O/sub 2/ evolution in Anacystis nidulans. United States.
Singh, D P, and Singh, S P. 1987. "Action of heavy metals on hill activity and O/sub 2/ evolution in Anacystis nidulans". United States.
@article{osti_6609676,
title = {Action of heavy metals on hill activity and O/sub 2/ evolution in Anacystis nidulans},
author = {Singh, D P and Singh, S P},
abstractNote = {Addition of 5 micromolar Cu/sup 2 +/, Cd/sup 2 +/, and Zn/sup 2 +/ was inhibitory to 10 micromolar H/sub 2/O/sub 2/-supported Hill activity (dichlorophenolindophenol reduction) and O/sub 2/ evolution in membrane preparation from Anacystis nidulans. The reversal of Cd/sup 2 +/ and Zn/sup 2 +/ inhibition, in contrast to Cu/sup 2 +/, by exogenously added catalase suggested that the former cations were inhibitory to H/sub 2/O/sub 2/ degradation. Ascorbic acid (20 micromolar) supported 27% of the Hill activity which was insensitive to DCMU (10 micromolar) and the remaining activity, attributable to the DCMU sensitive process, was sensitive to inhibition by Cu/sup 2 +/ only. It is suggestive that the action site of Cd/sup 2 +/ and Zn/sup 2 +/ is located between the electron donation sites of H/sub 2/O/sub 2/ and ascorbic acid, while that of Cu/sup 2 +/ is located beyond it. Electron donation by reduced glutathione was insensitive to DCMU and Cu/sup 2 +/, indicating that the action site of Cu/sup 2 +/ is prior to its electron donation site. Further, the phenanthroline (10 micromolar) reversal of Cu/sup 2 +/ inhibition of Hill activity suggested a tentative action site of Cu/sup 2 +/ at the level of cytochrome.},
doi = {},
url = {https://www.osti.gov/biblio/6609676}, journal = {Plant Physiol.; (United States)},
number = ,
volume = 83:1,
place = {United States},
year = {Thu Jan 01 00:00:00 EST 1987},
month = {Thu Jan 01 00:00:00 EST 1987}
}