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| - Resonance Raman Characterization of Soluble Guanylate Cyclase Expressed fromBaculovirus
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| - Resonance Raman spectra of the α1β1isoform of bovine lung soluble guanylate cyclaseexpressed from baculovirus have been measured. The spectra showthat the ferric heme is five-coordinatehigh spin whereas the ferrous heme in the absence of added exogenousligands is a mixture of six-coordinate low spin and five-coordinate high spin. In theFe−CO-derivative, the correlation between theFe−CO frequency (497 cm-1) and the C−Ofrequency (1959 cm-1) demonstrates that theproximal ligandin our preparation is histidine. The Fe−NO stretching frequency(found at 520 cm-1) and otherspectralfeatures of the ferrous Fe−NO-bound sGC are similar to those reportedby Deinum et al. () and Yu etal. (). These data indicate that although largepreparation-dependent differences in the occupancy of thedistal pocket exist, all the preparations have the same proximalhistidine ligation and share the samemechanism of activation by NO.
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