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• W1975486257 abstract "Resonance Raman (RR) spectra of cytochrome bd-type ubiquinol oxidase enriched with Fe-isotopes were investigated with excitation at 406.7, 424.0, 427.0, 441.6, and 647.1 nm. The bands of reduced form at 252 and 400 cm−1 were tentatively assigned to vFeHis of high-spin b595 and vFeMet of low-spin b558, respectively. The v and δFeOO bands of heme d-O2 were observed at 566 and ∼445 cm−1, respectively. The vFeCO frequency of heme d-CO was unusually low (477 cm−1) but the v4 frequency was not of P-450 type. Therefore, the axial ligand of heme d would not be an ordinary histidine or cysteine. © 1995 John Wiley & Sons, Inc." @default.
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• W1975486257 date "1995-01-01" @default.
• W1975486257 modified "2023-09-26" @default.
• W1975486257 title "Resonance raman study on axial ligands of heme irons in cytochromebd-type ubiquinol oxidase fromEscherichia coli" @default.
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• W1975486257 doi "https://doi.org/10.1002/bspy.350010502" @default.
• W1975486257 hasPublicationYear "1995" @default.
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