| Abstract;We placed the iron(II) complex of 2,7,12,17-tetraethyl-3,6,11,18-tetramethylcorrphycene, or etiocorrphycene, in myoglobin heme pocket. The reconstituted myoglobin was functionally active to reversibly bind gaseous ligands under physiological conditions. The partial pressures at half saturation for oxygen and carbon monoxide were P50=6.7 and 3.5mmHg, respectively. The affinities are one to two orders of magnitude lower than those reported for the native protein. The anomaly was ascribed to the geometric strain on the iron(II) atom in the trapezoidal coordination core of corrphycene. The above results further indicate that the peripheral carboxyl groups in corrphycene dicarboxylate account for 40% of the overall reduction in oxygen affinity, which has been reported for the myoglobin bearing bis(ethoxycarbonyl)corrphycenatoiron(II). (author abst.) |