Retention of cadmium in roots of maize seedlings: Role of complexation by phytochelatins and related thiol peptides

Abstract

Cd from roots of maize was partitioned in seedlings exposed to 3 μM CdSO4 for 1 to 7 d. Most of the root Cd (92-94%) was buffer soluble and provided the classical metal-induced cysteine-rich, high-molecular-weight Cd-binding complex. This complex, however, bound only part of the Cd within the roots, from 19% after 1 d of exposure to 59% by d 7. Three families of peptides formed the Cd-binding complex: (γ-glutamic acid-cysteine)n-glycine [(γ-GluCys)n-Gly], or phytochelatins, (γ-Glu-Cys)n, and (γ-Glu-Cys)n-Glu. The monothiols γ-Glu-Cys-Gly (glutathione), γ-Glu-Cys, and γ-GluCys-Glu were absent from the complex. The n2 oligomers of any peptide were the least concentrated, whereas the n3 and n4 oligomers increased in the complex with exposure to Cd. By d 7, 75% of (γ-Glu-Cys)4-Gly, 80% of (γ-Glu-Cys)4, and 73% of (γ-Glu-Cys)3-Glu were complexed with Cd. The peptide thiol:Cd molar ratio for the complexes was 1.01 ± 0.07, as if the minimal amount of thiol was used to bind Cd. Acid-labile sulfide occurred in the complexes from d 1 onward at the low S2-:Cd molar ratio of 0.18 ± 0.02.