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- W2497823897 abstract "Resonance Raman studies of Fe- and Cu-containing proteins have led to the identification of tyrosine, histidine, cysteine, and hydroxide ligands as well as Fe-O and Fe-S clusters. For the Fe-O clusters, the frequency and oxygen isotope dependence of the Fe-O-Fe symmetric stretch relates to Fe-O-Fe bond angle, while the peak intensity relates to the disposition of the other ligands in the cluster. For the Fe-S proteins, the frequencies and sulfur isotope dependence of the Fe-S vibrational modes can be used to distinguish mononuclear, binuclear, and tetranuclear clusters. Hydrogen bonding of both Fe-O and Fe-S clusters can be detected by frequency shifts in deuterium-substituted proteins." @default.
- W2497823897 created "2016-08-23" @default.
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- W2497823897 date "1988-06-21" @default.
- W2497823897 modified "2023-10-10" @default.
- W2497823897 title "Resonance Raman Spectroscopy of Iron—Oxo and Iron—Sulfur Clusters in Proteins" @default.
- W2497823897 doi "https://doi.org/10.1021/bk-1988-0372.ch003" @default.
- W2497823897 hasPublicationYear "1988" @default.
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