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. 1971 Oct;68(10):2532–2535. doi: 10.1073/pnas.68.10.2532

Differences between the Conformation of Arsanilazotyrosine 248 of Carboxypeptidase A in the Crystalline State and in Solution

Jack T Johansen 1, Bert L Vallee 1
PMCID: PMC389462  PMID: 5289887

Abstract

Coupling of carboxypeptidase A crystals with diazotized arsanilic acid specifically labels tyrosine 248, an active-site residue of the enzyme. Many azophenols are yellow and their zinc complexes are red; the “yellow” absorption spectrum of zinc arsanilazocarboxypeptidase crystals is characteristic of the arsanilazotyrosyl group, not of the zinc complex. This is consistent with the interpretation of x-ray data on native crystals of carboxypeptidase A, indicating that tyrosine 248 and the zinc atom are too far apart to form a complex. However, the enzyme in solution is red, denoting the formation of a complex between zinc and arsanilazotyrosine 248. The most likely interpretation of the data is that the orientation of arsanilazotyrosine 248 in solution and in the crystal is different. If the unlabeled tyrosine 248 of native carboxypeptidase undergoes similar changes, these data may bear upon the low activity of the enzyme in the crystalline state and on the catalytic mechanism of the enzyme based on the crystal structure. The opportunities for analogous spectrochemical studies of other, similar systems are pointed out.

Keywords: circular dichroism, azoprobe, visible spectrum

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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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