RIS ID

12474

Publication Details

Levy, J. L., Stauber, J. L., Adams, M., Maher, W., Kirby, J. K. & Jolley, D. F. (2005). Toxicity, biotransformation, and mode of action of arsenic in two freshwater microalgae (Chlorella sp. and Monoraphidium arcuatum). Environmental Toxicology and Chemistry, 24 (10), 2630-2639.

Abstract

The toxicity of As(V) and As(III) to two axenic tropical 15 freshwater microalgae, Chlorella sp. and Monoraphidium arcuatum, was determined using 72-h growth rate inhibition bioassays. Both organisms were tolerant to As(III) (72-h IC50, concentration to cause 50% inhibition of growth, of 25 and 15 mg As(III)/L, respectively). Chlorella sp. was also tolerant to As(V) with no effect on growth rate over 72 h at concentrations up to 0.8 mg/L (72-h IC50 of 25 mg As(V)/L). M. arcuatum was more sensitive to As(V) (72-h IC50 of 0.25 mg As(V)/L). An increase in phosphate in the growth medium (0.15 to 1.5 mg PO4 3- /L) decreased toxicity, i.e. the 72-h IC50 value for M. arcuatum increased from 0.25 mg As(V)/L to 4.5 mg As(V)/L, while extracellular As and intracellular As decreased, indicating competition between arsenate and phosphate for cellular uptake. Both microalgae reduced As(V) to As(III) in the cell, with further biological transformation to methylated species (monomethyl arsonic acid and dimethyl arsinic acid) and phosphate arsenoriboside. Less than 0.01% of added As(V) was incorporated into algal cells, suggesting that bioaccumulation and subsequent methylation was not the primary mechanism of detoxification. When exposed to As(V) both species reduced As(V) to As(III), however only M. arcuatum excreted As(III) into solution. Intracellular arsenic reduction may be coupled to thiol oxidation in both species. Arsenic toxicity was most likely due to arsenite accumulation in the cell, when the ability to excrete and/or methylate arsenite was overwhelmed at high arsenic concentrations. Arsenite may bind to intracellular thiols, such as glutathione, potentially disrupting the ratio of reduced to oxidised glutathione and consequently inhibiting cell division.

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Link to publisher version (DOI)

http://dx.doi.org/10.1897/04-580R.1