High-potential iron proteins derivatives

Fluorine-labeled analogues of C. vinosum high-potential iron protein have been investigated by F NMR spectroscopy. By incorporation of specific fluorine-labeled amino acid residues, one can insert unique probes at well-defined locations within the protein core. The synthesis and purification of 2-, 3-, and 4-fluorophenylalanine (abbreviated 2-F-, 3-F-, and 4-F-Phe, respectively), 3-fluorotyrosine (3-F-Tyr), and 5-fluorotr3q)tophan (5-F-Trp) derivatives of C. vinosum HiPIP, the assignment of F NMR resonances, the measurement of longitudinal relaxation times, and the temperature dependence of F and resonances have all been reported 42, 43, 136). These measurements were used to examine structural perturbations of mutants, the dynamics of interaction of residues with the cluster, and solvent accessibility, and as a test of the relative contribution of cross-relaxation to magnetization decay. 

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