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Summary: The soluble cytochrome oxidase/nitrite reductase of Nitrosomonas europaea, induced under low O2 tensions, has a high affinity for O2. EPR spectroscopy indicates that this enzyme contains 'type I' ('blue') and ('type II') Cu2+-sites, and UV/visible spectroscopy suggests the presence of a ('type III') Cu2+-pair. The enzyme binds exogenous copper in an unusual way, resulting in modified EPR spectra and a very high εM for the 'blue' 598 nm absorption band when low levels of Cu2+ (10 μM) are present during purification.
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