Abstract:
:The oxygen reaction of Nitrosomonas europaea cytochrome c oxidase containing either 2Cu or 1Cu per two heme a molecules was investigated by the flow-flash technique at 20 degrees C. The reaction profiles of the bacterial enzyme were essentially the same as those of bovine heart cytochrome c oxidase, although the rate of the primary oxygen compound formation was much slower. The 1Cu enzyme exhibited higher rates for both primary oxygen compound formation and intramolecular electron transfer than the 2Cu enzyme. This result clearly indicates that CuA is not essential functionally for the oxidation of ferrous heme a moieties, and suggests its structural importance in maintaining the molecular integrity of N. europaea cytochrome oxidase.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Orii Y,Sakamoto T,Fukumori Y,Yamanaka Tdoi
10.1016/0006-291x(92)91868-qsubject
Has Abstractpub_date
1992-02-14 00:00:00pages
1264-9issue
3eissn
0006-291Xissn
1090-2104pii
0006-291X(92)91868-Qjournal_volume
182pub_type
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