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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...
The bacterial quinol oxidase, cytochrome o, is an enzyme which is highly analogous to the better known cytochrome c oxidase, cytochrome aa 3 but with the important difference that it lacks the near infra-red absorbing pigment Cu A . In this article we report an absorption band in the near IR spectrum of cytochrome o with a maximal absorption at 738 nm, and which is attributable to...
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