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EPR spectroscopy of Escherichia coli cytochrome bo which lacks Cu B
Author(s) -
Hunter Dominic J.B,
Moody A.John,
Rich Peter R,
Ingledew W.John
Publication year - 1997
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/s0014-5793(97)00735-7
Subject(s) - escherichia coli , electron paramagnetic resonance , chemistry , spectroscopy , cytochrome b , cytochrome , copper , crystallography , biochemistry , nuclear magnetic resonance , physics , enzyme , gene , organic chemistry , quantum mechanics , mitochondrial dna
The spectroscopic and ligand‐binding properties of a copper‐deficient cytochrome bo 3 , a member of the haem–copper superfamily of terminal oxidases, are reported and contrasted with those of the native enzyme. The enzyme lacks the copper atom (Cu B ) which is normally an integral part of the catalytic site. The consequences of loss of the Cu B are the loss of antiferromagnetic coupling to the high‐spin haem and an inability to form any of the integer‐spin derivatives of the enzyme. Low‐spin compounds of the normally high‐spin haem are still formed with appropriate ligands, although these are modified.