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Fructose-induced modifications of myoglobin: Change of structure from met (Fe3+) to oxy (Fe2+) form
Abhishek Bhattacherjee1, Abhay Sankar Chakraborti
1Department of Biophysics, Molecular Biology and Bioinformatics, University College of Science, 92, Acharya Prafulla Chandra Road, Kolkata 700009, India.
Abstract:
We studied structural modifications of metmyoglobin (Mb) after short-term (6 days) and long-term (30 days) glycation by fructose (fructation). Fructation caused gradual changes in the structure of the protein with respect to increased absorbance at 280 nm, enhanced fluorescence emission (with excitation at 285 nm), increased surface accessible tryptophan residues and reduced α-helix content and change in tertiary structure. However, long-term fructation changed Mb to oxymyoglobin (MbO2), as demonstrated by different spectroscopic (absorption, fluorescence, circular dichroic and electron paramagnetic resonance) studies and trifluoperazine-induced oxygen release experiment. Fructation appeared to modify Arg139 to arg-pyrimidine, which exhibited antioxidative activity and might be involved in the conversion of met (Fe3+) to oxy (Fe2+) form of myoglobin.
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