Resonance Raman spectroscopy of amicyanin, a blue copper protein from Paracoccus denitrificans.

Resonance Raman spectroscopy of amicyanin, a blue copper protein from Paracoccus denitrificans.

The copper binding site of amicyanin from Paracoccus denitrificans has been examined by resonance Raman spectroscopy. The pattern of vibrational modes is clearly similar to those of the blue copper proteins azurin and plastocyanin. Intense resonance-enhanced peaks are observed at 377, 392, and 430 cm-1 as well as weaker overtones and combination bands in the high frequency region. Most of the p...

An inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties, and physiological role.

When grown on methylamine as a sole carbon source, Paracoccus denitrificans synthesizes a Type I blue copper protein which mediates electron transfer between methylamine dehydrogenase and cytochrome c. This blue copper protein does not serve as an electron acceptor for methanol dehydrogenase and is not synthesized by cells grown on methanol or succinate. The blue copper protein and methylamine ...

An engineered CuA Amicyanin capable of intermolecular electron transfer reactions.

The type I copper center of amicyanin was replaced with a binuclear CuA center. To create this model CuA protein, a portion of the amino acid sequence that contains three of the ligands to the native type I copper center of Paracoccus denitrificans amicyanin was replaced with the corresponding portion of sequence that provides five ligands for the CuA center of cytochrome c oxidase from P. deni...

THE EFFECTS OF COPPER ON CYTOCHROMES BIOSYNTHESIS, CELL DIVISION IWD MUTAGENESIS IN PARACOCCUS DENITRIFICANS

EXAFS analysis of the pH dependence of the blue-copper site in amicyanin from Thiobacillus versutus.

The room temperature Cu K-edge EXAFS (extended X-ray absorption fine structure) spectrum of reduced and oxidized amicyanin, the blue copper protein from Thiobacillus versutus, was measured at low and high pH. The data interpretation was partly based on independent NMR evidence for the occurrence of a ligand histidine protonation at low pH (pKa = 6.9) in the reduced protein. In the oxidized prot...