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. 1980 Sep;77(9):5028–5031. doi: 10.1073/pnas.77.9.5028

Coordination environment and fluoride binding of type 2 copper in the blue copper protein ascorbate oxidase

John H Dawson 1,*, David M Dooley 1,†, Harry B Gray 1,‡
PMCID: PMC349986  PMID: 16592868

Abstract

The coordination environment of the type 2 (nonblue) copper in native ascorbate oxidase (L-ascorbate:oxygen oxidoreductase, EC 1.10.3.3) and of a derivative of the enzyme having the type 1 (blue) copper reversibly bleached has been examined by electron paramagnetic resonance (EPR) spectroscopy. In the g[unk] region of the spectrum of bleached ascorbate oxidase, a seven-line superhyperfine pattern is seen that is attributed to the presence of three nitrogen-donor ligands to a type 2 copper having tetragonal geometry. The superhyperfine splitting patterns in the g∥ region of the EPR spectra of native and bleached ascorbate oxidase show that as many as two fluorides may bind to type 2 copper. Because fluoride inhibits the enzyme competitively with respect to ascorbic acid, it is proposed that the type 2 copper is part of the ascorbate binding site.

Keywords: nonblue copper, electron paramagnetic resonance, square planar geometry, nitrogenous ligands

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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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