Partial purification and characterization of a soluble haemoprotein, having spectral properties similar to cytochrome a 1, from anaerobically grown Escherichia coli

FEBS Letters

Baines, Baldev S.¹  Poole, Robert K.¹  Williams, Huw D.¹  Hubbard, Julia A.M.² 

[1]Departments of Microbiology, University of London, Campden Hill, London W8 7AH, England

[2]Chemistry, Queen Elizabeth College, University of London, Campden Hill, London W8 7AH, England

关键词: Cytochrome a 1;    Catalase;    Peroxidase;    Escherichia coli;    Bacterial electron transport;    Anaerobic respiration;   

DOI  :  10.1016/0014-5793(84)80510-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

‘Soluble’ fractions obtained after high-speed differential centrifugation of extracts from ultrasonically disrupted Escherichia coli, grown anaerobically with glycerol and fumarate, contain at least two haemoproteins, distinguishable by their CO-binding characteristics. Reduced minus oxidized spectra show a maximum at 598 nm and a shoulder to the Soret region near 440 nm, features generally attributed to ‘cytochrome a ₁’. CO-reduced minus reduced difference spectra show the more rapidly CO-binding component to have a trough at 444 nm, also generally attributable to an a-type cytochrome. The partially purified a ₁-like component has catalase and peroxidase activities, and lacks copper. An appropriate nomenclature for the a ₁-like haemoprotein and its similarity to catalase are discussed.

【 授权许可】

Unknown