Solution of 1h nmr structure of the heme cavity in the oxygen-avid myoglobin from the trematode paramphistomum epiclitum*

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  • who: Wei Zhang from the tion where it could provide the second hydrogen bond to the bound oxygen, as well as form a hydrogen bond to the Tyr(B10) hydroxyl oxygen to stabilize the optimal orientations of both Tyr32(B10) and Tyr66(E7) for hydrogen bonding to O The role of both Tyr32(B10) and Tyr66(E7) hydroxyl protons in forming hydrogen bonds to the ligand is independently supported by the very slow exchange rate with bulk water, with estimated lifetime have published the research work: Solution of 1H NMR Structure of the Heme Cavity in the . . .

     

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