Proton nuclear magnetic resonance study of the dynamic stability of the heme pocket of soybean leghemoglobin a. Exchange rates for the labile proton of the proximal histidyl imidazole.
作者： S B Kong , J D Cutnell , G N La Mar
DOI: 10.1016/S0021-9258(18)32743-1
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摘要: Intrinsic spin lattice relaxation times for the hyperfine-shifted exchangeable resonances and downfield heme methyls low met-cyano-, met-nicotinate-, deoxy- complexes of soybean leghemoglobin a were determined in H2O. When exchange with bulk solvent is slow on T1 time scale, comparison intrinsic values protons methyl has provided assignment proximal histidyl imidazole N1H proton resonance. Transfer saturation experiments linewidth data as function pH at 25 degrees C permitted determination rates various protein oxidation/ligation states. The found to be base-catalyzed well met-azide- complexes. are taken measures magnitude fluctuations conformation near cavity. unligated deoxy-protein exhibited greater kinetic stability than ligated forms protein, bulky nicotinate ligand resulted lowest forms. In contrast met-cyanomyoglobin, no resonance which could attributed distal NH was observed any leghemoglobin. Comparison between same form myoglobin reveals that former exhibits an order faster latter both states, confirming flexibility pocket
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