TY - JOUR
T1 - Resonance raman study on axial ligands of heme irons in cytochrome bd‐type ubiquinol oxidase from Escherichia coli
AU - Hirota, Shun
AU - Mogi, Tatsushi
AU - Anraku, Yasuhiro
AU - Gennis, Robert B.
AU - Kitagawa, Teizo
PY - 1995
Y1 - 1995
N2 - 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 vFeHis of high‐spin b595 and vFeMet of low‐spin b558, respectively. The v FeO 2 and δFeOO bands of heme d‐O2 were observed at 566 and ∼445 cm−1, respectively. The vFeCO 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.
AB - 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 vFeHis of high‐spin b595 and vFeMet of low‐spin b558, respectively. The v FeO 2 and δFeOO bands of heme d‐O2 were observed at 566 and ∼445 cm−1, respectively. The vFeCO 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.
UR - http://www.scopus.com/inward/record.url?scp=84984233402&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84984233402&partnerID=8YFLogxK
U2 - 10.1002/bspy.350010502
DO - 10.1002/bspy.350010502
M3 - Article
AN - SCOPUS:84984233402
VL - 1
SP - 305
EP - 311
JO - Biopolymers
JF - Biopolymers
SN - 0006-3525
IS - 5
ER -