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- W2047906858 abstract "The axial ligands of low potential cytochrome b560 in the five subunit bovine heart succinate-ubiquinone reductase complex and in the isolated quinone binding proteins have been investigated using EPR and near-infrared magnetic circular dichroism spectroscopies. The results are consistent with bis-histidine ligation with near-perpendicular imidazole rings for cytochrome b560 in the four-subunit complex. The pronounced changes in EPR properties that accompany isolation of the cytochrome-b560 containing quinone binding proteins, are attributed to perturbation of the orientation of the imidazole rings of the heme bis-histidine ligands, rather than a change in axial ligation." @default.
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- W2047906858 date "1995-06-19" @default.
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- W2047906858 title "Spectroscopic identification of the axial ligands of cytochrome<i>b</i><sub>560</sub>in bovine heart succinate-ubiquinone reductase" @default.
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- W2047906858 doi "https://doi.org/10.1016/0014-5793(95)00522-b" @default.
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