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. 1984 Apr;45(4):755–766. doi: 10.1016/S0006-3495(84)84219-8

The accessibility of type I Cu(II) centers in laccase, azurin, and stellacyanin to exchangeable hydrogen and ambient water.

W B Mims, J L Davis, J Peisach
PMCID: PMC1434907  PMID: 6326878

Abstract

The characteristic deuterium modulation pattern was observed in the electron spin-echo envelopes for laccase, decupro laccase (from which Type 2 copper had been removed), stellacyanin, and azurin that had been exchanged against D2O. From the decay rate of the modulation pattern and from a quantitative analysis of the modulation depth, we conclude that the Cu(II) sites in these proteins are directly accessible to solvent. Similar results were obtained for laccase and decupro laccase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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