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Article

The structural role of the copper-coordinating and surface-exposed histidine residue in the blue copper protein azurin.

Journal of molecular biology - 9 Jun 2000

Jeuken L J, Ubbink M, Bitter J H, van Vliet P, Meyer-Klaucke W, Canters G W

Abstract excerpt

Copper K-edge extended X-ray absorption fine structure (EXAFS) spectroscopy and (15)N NMR relaxation studies were performed on samples of a variant azurin in which the surface-exposed histidine ligand of the copper atom (His117) has been replaced by glycine. The experiments were performed to probe the structure of the active site and the protein dynamics. The cavity in the protein structure created by the...

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Identifiers

PMID: 10835281
DOI: 10.1006/jmbi.2000.3754

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The structural role of the copper-coordinating and surface-exposed histidine residue in the blue copper protein azurin.PMID 10835281Read ↗

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