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The hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 (GlbN) contains three tyrosines (Tyr5, Tyr22, and Tyr53), each of which undergoes a structural rearrangement when the protein binds an exogenous ligand such as cyanide. We explored the use of 3‐fluorotyrosine and 19F‐NMR spectroscopy for the characterization of GlbN. Assignment of 19F resonances in fluorinated GlbN (GlbN*) was achieved...
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