Resonance Raman spectroscopy of an oxygenated intermediate species of cytochrome oxidase d from Escherichia coli

FEBS Letters

Campbell, N.J.²  Hubbard, J.A.M.¹  Poole, R.K.³  Hughes, M.N.¹  Baines, B.S.³ 

[1] Department of Chemistry, Queen Elizabeth College, Campden Hill, London, W8 7AH England;Department of Chemistry, Imperial College, London SW7 2AY, England;Department of Microbiology, Queen Elizabeth College, Campden Hill, London W8 7AH England

关键词: Raman spectroscopy;    Oxygen reaction;    Cytochrome oxidase;    Bacterial respiration;   

DOI  :  10.1016/0014-5793(82)81323-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Resonance Raman spectroscopy (excitation at 647.1 nm) of solubilized and aerated cytochrome oxidase d from Escherichia coli K12 has shown absorptions (1078–1105 cm⁻¹) attributed to the oxygen—oxygen stretching frequency of the oxidase—oxygen adduct. These findings support the hypothesis that the 650–652 nm chromophore of cytochrome d is an oxygenated or ’oxy’ intermediate species and not the fully oxidized enzyme.

【 授权许可】

Unknown