1887

Abstract

SUMMARY: The soluble cytochrome oxidase of has been highly purified and shown to be a copper protein devoid of haem, not a cytochrome as was previously assumed. The native molecular weight was 120000 and the subunit molecular weight 35000. Soluble cytochrome oxidase activity co-purified with nitrite reductase activity; both activities were almost certainly associated with the same protein. The possible physiological role of the nitrite reductase activity is discussed.

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/content/journal/micro/10.1099/00221287-129-6-1645
1983-06-01
2019-10-20
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-129-6-1645
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