1H and 2H ENDOR Investigations of Flavin Radicals Bound to Riboflavin Binding Protein from Egg White

Riboflavin-binding apoprotein isolated from egg white has been used as a protein matrix for a variety of substituted and/or deuterated flavins. The neutral radical states of the reconstituted flavoproteins were studied by ENDOR (electron nuclear double resonance) spectroscopy in disordered solids. For the first time all major hyperfine coupling constants of a flavin cofactor embedded within a protein could be measured and unambiguously assigned to molecular positions. Some conclusions about the geometrical arrangement of the flavin within the protein pocket and about molecular motions could be drawn.

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