Heme environment in aldoxime dehydratase involved in carbon–nitrogen triple bond synthesis
2004; Wiley; Volume: 568; Issue: 1-3 Linguagem: Inglês
10.1016/j.febslet.2004.05.008
ISSN1873-3468
AutoresKen-Ichi Oinuma, Takehiro Ohta, Kazunobu Konishi, Yoshiteru Hashimoto, Hiroki Higashibata, Teizo Kitagawa, Michihiko Kobayashi,
Tópico(s)Heme Oxygenase-1 and Carbon Monoxide
ResumoResonance Raman spectra have been measured to characterize the heme environment in aldoxime dehydratase (OxdA), a novel hemoprotein, which catalyzes the dehydration of aldoxime into nitrile. The spectra showed that the ferric heme in the enzyme is six‐coordinate low spin, whereas the ferrous heme is five‐coordinate high spin. We assign a prominent vibration that occurs at 226 cm −1 in the ferrous enzyme to the Fe‐proximal histidine stretching vibration. In the CO‐bound form of OxdA, the correlation between the Fe–CO stretching (512 cm −1 ) and C–O stretching (1950 cm −1 ) frequencies also supports our assignment of proximal histidine coordination.
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