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Spectral properties of a cyanobacterial cytochrome c oxidase evidence for cytochrome aa 3


Biochemical & Biophysical Research Communications 98(1): 72-79
Spectral properties of a cyanobacterial cytochrome c oxidase evidence for cytochrome aa 3
Membranes isolated from Nostoc sp. strain Mac oxidized NAD(P)H and horse heart ferrocytochrome c in dark reactions inhibited by KCN, NaN3, CO and by anaerobiosis. Reduced minus oxidized difference spectra revealed peaks at 603 and 445 nm which shifted to 590 and 430 nm, respectively, in reduced plus CO minus reduced spectra. In the presence of suitable electron mediators the pigment was reduced with NAD(P)H or ascorbate; KCN prevented this reduction. Photoaction spectra of CO-inhibited membranes showed peaks at 590 and 430 nm. Cytochrome aa3 apparently is a functional respiratory oxidase in Nostoc sp. strain Mac.

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Accession: 006459760

PMID: 6260105



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