The structural role of the copper-coordinating and surface-exposed histidine residue in the blue copper protein azurin 1 1Edited by R. Huber
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference75 articles.
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2. Raman spectroscopy as an indicator of Cu-S bond length in type 1 and type 2 copper cysteinate proteins;Andrew;J. Am. Chem. Soc.,1994
3. Cysteine ligand vibrations are responsible for the complex resonance Raman spectrum of azurin;Andrew;J. Biol. Inorg. Chem.,1997
4. Structure of azurin from Alcaligenes denitrificans refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules;Baker;J. Mol. Biol.,1988
5. X-ray absorption edge spectroscopy of copper(I) complexes. Coordination geometry of copper(I) in the reduced forms of copper proteins and their derivatives with carbon monoxide;Blackburn;Inorg. Chem.,1989
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