Abstract
Nitrophorins (NPs) occur in the blood-sucking insect Rhodnius prolixus. These proteins use ferric heme to store nitric oxide (NO) in the salivary glands of the insects and transport it to the victim’s tissues, resulting in vasodilation and reduced blood coagulation. In this work we present a nuclear inelastic scattering (NIS) study in order to characterize the iron-NO interaction in the isoform nitrophorin 7 (NP7). The NIS data obtained for NP7 complexed with NO show a strong band at ∼589 cm−1 which is due to modes with significant Fe-NO stretching and bending character. Another conspicuous feature is a significant peak at ∼280 cm−1 in the region where the heme modes occur. Based on a hybrid calculation method, which uses density functional theory and molecular mechanics, the band at ∼280 cm−1 is assigned to heme modes with substantial doming character.
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