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Abstract
Tin protoporphyrin IX (SnPP) is being used in the treatment of hyperbilirubinemia. We have studied the SnPP complex with equine myoglobin (EqMb) by 1H and 119Sn nuclear magnetic resonance spectroscopy (NMR) as a general model for SnPP interaction with hemoproteins. The complex formed from SnPP and EqMb, SnPP.EqMb, was found to have essentially the same porphyrin-binding pocket as EqMbCO, including the same porphyrin orientation in the major form of EqMbCO. 119Sn NMR spectroscopy has been used to demonstrate that the proximal His93F8-metal coordination is likely to be intact in SnPP.EqMb. Minor shifts in the side chain positions of some of the residues are indicated, possibly reflecting the presence of water in the sixth coordination site. SnPP.EqMb appears to be stable; it persists at room temperature for weeks and exhibits very slow exchange rates (2H for 1H) for a large number of amide protons in the pH range 7-9.
Highlights
Tin protoporphyrin IX (SnPP) is being used in the treatment of hyperbilirubinemia
We have studied the SnPP complex with equine myoglobin (EqMb) by 'H and "'Sn nuclear magnetic resonance spectroscopy (NMR) as a general model for SnPP interaction with hemoproteins.The complex formedfrom SnPP and EqMb, SnPP-EqMb,was found tohave essentially the same porphyrin-bindingpocket as EqMbCO, including the same porphyrin orientation in the major form of EqMbCO."'SnNMR spectroscopy has been usedto demonstrate that the proximal H i ~ ~ ~ F S - m ectoaolrdination is likely to be intact in SnPP-EqMb
An 'H NMR analysisof the complex of zinc protoporphyrin IX with leghemoglobin (ZnPP'-leghemoglobin) has been reported (Daelvt aitl., 1986), as has a " T d NMR analysis of CdPP
Summary
Tin protoporphyrin IX (SnPP) is being used in the treatment of hyperbilirubinemia. We have studied the SnPP complex with equine myoglobin (EqMb) by 'H and "'Sn nuclear magnetic resonance spectroscopy (NMR) as a general model for SnPP interaction with hemoproteins.The complex formedfrom SnPP and EqMb, SnPP-EqMb,was found tohave essentially the same porphyrin-bindingpocket as EqMbCO, including the same porphyrin orientation in the major form of EqMbCO."'SnNMR spectroscopy has been usedto demonstrate that the proximal H i ~ ~ ~ F S - m ectoaolrdination is likely to be intact in SnPP-EqMb. Resonance Assignment Strategy-Fig. 1, A and B , shows the major and minor porphyrin insertion isomers that have been found for native Mb (La Mar etal., 1983). For SnPP .EqMb there are four downfield resonances that correspond to the four meso-proton resonances
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