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May 1, 2026ChemPhysChem0 citationsOpen Access

Transient Absorption Spectroscopy of Blue Copper Sites in Divergent Protein Folds: Azurin Versus Multicopper Oxidase

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LDLuis I. DomenianniPKPatrycja Kielb

Key Points

  • The study aims to understand how structural differences in proteins affect energy relaxation pathways in blue copper sites.
  • Utilized transient absorption spectroscopy to analyze azurin and multicopper oxidase.
  • Investigated structural rigidity and coordination constraints related to blue copper sites.
  • Identified differences in ultrafast energy relaxation pathways based on protein arrangement.
  • Results indicate conserved metal coordination is influenced by surrounding structural factors.

Abstract

for azurin. These differences are correlated with variations in structural rigidity and coordination constraints beyond the first coordination spheres of the blue copper site. Our results reveal that, despite conserved metal coordination, the surrounding protein arrangement plays a significant role in shaping ultrafast energy relaxation pathways in metalloprotein.

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Cite This Study

Domenianni et al. (2026) studied this question.

synapsesocial.com/papers/69f443e8967e944ac5566fbchttps://doi.org/10.1002/cphc.202500924
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