Interactions of chromium (III) and chromium (VI) with bovine serum albumin studied by UV spectroscopy, circular dichroism, and fluorimetry.

In the present work, the interactions of bovine serum albumin (BSA) with chromium (III) chloride, potassium dichromate, and chromate were studied by fluorescence, circular dichroism, and UV-vis absorbance spectroscopy. Fluorescence quenching of BSA by chromium (III) was found to be a dynamic process in the beginning, turning static at later stages. Spectroscopic data show that both dichromate and chromate bind in similar electrostatic fashion to BSA and does not follow the fluorescence quenching observation for chromium (III).