ISSN:
1432-072X
Keywords:
Copper-limitation
;
Escherichia coli
;
Cytochrome oxidases
;
Oxygen reduction
;
Respiratory chains
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract The role(s) of copper in a bacterial cytochrome oxidase of the aa 3-type was investigated by growth of Paracoccus denitrificans NCIB 8944, in batch and steady state continuous culture, in a medium from which the bulk of the copper had been extracted. In a medium containing approximately 0.02 μM copper, cellular copper content, cytochromes a+a 3 and cytochrome a 3 were reduced to 55%, 58% and 33% respectively of control values and there were also less marked decreases in cytochromes c+c 1 (to 85%) and a CO-binding b-type cytochrome, possibly cytochrome o (to 71%). Copper deficiency elicited in reduced minus oxidized difference spectra a shift to shorter wavelengths and narrowing of the band width of the α-band of the oxidase, and loss of a (negative) band near 830 nm attributable to CuA (the copper functionally associated with haem a in the oxidase complex). The oxidase in copper-deficient cells reacted with oxygen to form the oxy “Compound A” at rates similar to that in control cells but CO recombination to ferrous haem a 3 was slowed 4-fold in the copper deficient case. The results are interpreted as indicating loss of CuA and changes in the proportions of haems a and a 3 with retention of catalytic activity. Titrations of respiration rates with antimycin suggested that copper deficiency did not result in diversion of electron flux through an antimycin A-insensitive, cytochrome o-terminated branch of the respiratory chain.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00406555
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