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- W2017059042 abstract "The iron complex of pyropheophorbide a methyl ester, 1, and 2-devinylpyropheophorbide a methyl ester, 2, have been reconstituted into equine myoglobin, Mb. The 1 H NMR spectra of the resulting protein complexes indicate that the chlorins are incorporated into the heme pocket in a manner similar to that of the native heme. The 1 H NMR spectra of the cyano-met Mb complex containing 1 and 2 are shown to be heterogeneous. In the complex of 1, three species could be identified and labeled A, B, and C with equilibrium ratios at 5 o C of 1.0:0.4:0.04, respectively" @default.
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- W2017059042 date "1992-07-01" @default.
- W2017059042 modified "2023-10-05" @default.
- W2017059042 title "Proton NMR study of the molecular and electronic structure of paramagnetic iron chlorin complexes of myoglobin: dynamic heterogeneity of the heme pocket" @default.
- W2017059042 doi "https://doi.org/10.1021/ja00042a035" @default.
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