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Partial purification and characterization of a soluble haemoprotein, having spectral properties similar to cytochrome a 1 , from anaerobically grown Escherichia coli
Author(s) -
Baines Baldev S.,
Williams Huw D.,
Hubbard Julia A.M.,
Poole Robert K.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80510-4
Subject(s) - chemistry , hemeprotein , cytochrome , peroxidase , escherichia coli , catalase , heme , biochemistry , cytochrome c peroxidase , cytochrome c , chromatography , stereochemistry , enzyme , mitochondrion , gene
‘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.