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The formate complex of the cytochrome bo quinol oxidase of Escherichia coli exhibits a ‘g = 12’ EPR feature analogous to that of ‘slow’ cytochrome oxidase
Author(s) -
Calhoun Melissa W.,
Gennis Robert B.,
Salerno John C.
Publication year - 1992
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(92)81079-2
Subject(s) - cytochrome c oxidase , cytochrome , chemistry , heme , cytochrome b , oxidase test , protein subunit , escherichia coli , heme a , cytochrome p450 reductase , cytochrome c1 , cytochrome c , cytochrome c peroxidase , coenzyme q – cytochrome c reductase , biochemistry , formate dehydrogenase , formate , stereochemistry , enzyme , catalysis , mitochondrion , gene , mitochondrial dna
The cytochrome bo quinol oxidase of Escherichia coli is homologous in sequence and in structure to cytochrome aa 3 type cytochrome oxidase in subunit 1, which contains the catalytic core. The cytochrome bo enzyme forms a formate complex which exhibits ‘g = 12’ and ‘g = 2.9’ EPR signals at X band; similar signals have previously been observed only in association with the ‘slow’ and formate‐ligated states of cytochrome oxidase. These signals arise from transitions within integral spin multiplets identified with the homologous heme‐copper binuclear catalytic centers in both enzymes.