1988 Volume 1988 Issue 4 Pages 425-430
The copper-containing dissimilatory nitrite reductase [nitrogen monoxide: ferricytochrome coxidoreductase, EC 1.7.2.1] was purified from a denitrifying phototropic b acterium, Rhodopseudonzonas sphaeroides forma sp. denitrificans, and its absorption spectrum (Fig.2)showed absorption maxima at 592 and 458 nm with broad shoulders at wavelength longer than 600 nm and a shoulder at 393 nm. Its CD spectrum showed positive peaks at 830, 555, and 394 nm and strong negative peaks at 680 and 463 nm. The two CD peaks at the longest wavelength are assigned to splitted S(π)→dx2-2 charge-transfer transitions. The ESR parameters of signals due to the type I and type II Cu(II) centers showed small pH dependency (Fig.3) which corresponds to the, pH-dependency of cytochrome c oxidase activity of this enzyme.
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