The complexation with proteins in extracellular polymeric substances alleviates the toxicity of Cd (II) to Chlorella vulgaris.

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Summary of "The complexation with proteins in extracellular polymeric substances alleviates the toxicity of Cd (II) to Chlorella vulgaris."

The complexation with extracellular polymeric substances (EPS) greatly reduces the toxicity of heavy metals towards organisms in the environment. However, the molecular mechanism of EPS-metal complexation remains unclear owing to the limitation of precise analysis for key fractions and functionalities in EPS that associate with metals. Herein, we explored the EPS-Cd (II) complexation by fluorescence excitation emission matrix coupled with parallel factor (EEM-PARAFAC), two-dimensional Fourier transform infrared correlation spectroscopy (2D-FTIR-COS) and X-ray photoelectron spectroscopy (XPS), attempting to explain the mechanisms of EPS in alleviating Cd (II) toxicity toward a green alga Chlorella vulgaris (C. vulgaris). When the algal EPS were removed, the cell internalizations of Cd (II), growth inhibition rate and chlorophyll autofluorescence increased, but the surface adsorption and esterase activities decreased, indicating that the sorption of Cd (II) by EPS was crucial in alleviating the algal toxicity. Moreover, the complexation with proteins in EPS controlled the sorption of Cd (II) to algal EPS, resulting in the chemical static quenching of the proteins fluorescence by 47.69 ± 2.37%. Additionally, the complexing capability of the main functionalities, COO and C-OH in proteins with Cd (II) was stronger than that of C-O(H) and C-O-C in polysaccharides or C-OH in the humus-related substances. Oxygen atom in protein carboxyl C-O might be the key site of EPS-Cd (II) complexation, supported by the modified Ryan-Weber complexation model and the obvious shift of oxygen valence-electron signal. These findings provide deep insights into understanding the interaction of EPS with heavy metals in aquatic environment.


Journal Details

This article was published in the following journal.

Name: Environmental pollution (Barking, Essex : 1987)
ISSN: 1873-6424
Pages: 114102


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Medical and Biotech [MESH] Definitions

A technique for measuring extracellular concentrations of substances in tissues, usually in vivo, by means of a small probe equipped with a semipermeable membrane. Substances may also be introduced into the extracellular space through the membrane.

Macromolecular organic compounds that contain carbon, hydrogen, oxygen, nitrogen, and usually, sulfur. These macromolecules (proteins) form an intricate meshwork in which cells are embedded to construct tissues. Variations in the relative types of macromolecules and their organization determine the type of extracellular matrix, each adapted to the functional requirements of the tissue. The two main classes of macromolecules that form the extracellular matrix are: glycosaminoglycans, usually linked to proteins (proteoglycans), and fibrous proteins (e.g., COLLAGEN; ELASTIN; FIBRONECTINS; and LAMININ).

A 15 kD "joining" peptide that forms one of the linkages between monomers of IMMUNOGLOBULIN A or IMMUNOGLOBULIN M in the formation of polymeric immunoglobulins. There is one J chain per one IgA dimer or one IgM pentamer. It is also involved in binding the polymeric immunoglobulins to POLYMERIC IMMUNOGLOBULIN RECEPTOR which is necessary for their transcytosis to the lumen. It is distinguished from the IMMUNOGLOBULIN JOINING REGION which is part of the IMMUNOGLOBULIN VARIABLE REGION of the immunoglobulin light and heavy chains.

PROTEOGLYCANS-associated proteins that are major components of EXTRACELLULAR MATRIX of various tissues including CARTILAGE; and INTERVERTEBRAL DISC structures. They bind COLLAGEN fibers and contain protein domains that enable oligomer formation and interaction with other extracellular matrix proteins such as CARTILAGE OLIGOMERIC MATRIX PROTEIN.

Specialized Fc receptors (RECEPTORS, FC) for polymeric immunoglobulins, which mediate transcytosis of polymeric IMMUNOGLOBULIN A and IMMUNOGLOBULIN M into external secretions. They are found on the surfaces of epithelial cells and hepatocytes. After binding to IMMUNOGLOBULIN A, the receptor-ligand complex undergoes endocytosis, transport by vesicle, and secretion into the lumen by exocytosis. Before release, the part of the receptor (SECRETORY COMPONENT) that is bound to IMMUNOGLOBULIN A is proteolytically cleaved from its transmembrane tail. (From Rosen et al., The Dictionary of Immunology, 1989)

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