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Spectral properties of the leucine iso leucine valine binding protein and its complexes with substrates

, : Spectral properties of the leucine iso leucine valine binding protein and its complexes with substrates. Soviet Journal of Bioorganic Chemistry 7(1): 35-46

The difference UV, fluorescence, CD [circular dichroism] and Raman spectra were studied for Escherichia coli leucine-isoleucine-valine binding protein (LIV-protein), for LIV-protein depleted from endogeneous substrates (s-LIV-protein), and for complexes of these 2 proteins with leucine and isoleucine. The s-LIV-protein complex shows altered spectral parameters of the aromatic residues (tryptophan and tyrosine) of the proteins. The protein has at least 2 substrate binding sites which differ in their affinity. The high-affinity site contains 1 tryptophan residue and, possibly, 1 tyrosine residue. A hypothetical model for the substrate binding by LIV-protein is suggested.

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