Work

X-ray absorption spectroscopy of folded and unfolded copper(I) azurin

Year: 2000

Type: article

Abstract: The structure of the copper site in folded and unfolded copper(I) azurin has been investigated by X-ray absorption spectroscopy (XAS). Analysis of the Cu K-edge spectra demonstrates that Cu(I) occupies a trigonal coordination site in the unfolded protein; and EXAFS data indicate a structure with 1.5–2 CuS(Cl) and 1.5–1 CuN(O) bonds. It is likely that the cysteine S and one of the two histidine N atoms remain coordinated in the unfolded structure, and that the third ligand is S(Met) or Cl−. The lengths of both the CuS(Cys) and CuN(His) bonds increase by ∼0.1 Å on unfolding, in accord with the view that copper coordination is constrained by the protein.

Source: Inorganica Chimica Acta

DOI: 10.1016/s0020-1693(99)00315-1

Authors: Serena DeBeer, Pernilla Wittung-Stafshede, Johan Leckner, Göran Karlsson, Jay R Winkler, Harry B Gray, Bo G Malmström, Edward I Solomon, Britt Hedman, Keith O Hodgson

Institutions: Stanford University, California Institute of Technology, University of Gothenburg, SLAC National Accelerator Laboratory, Stanford Synchrotron Radiation Lightsource

Language: English

Topic: X-ray Spectroscopy and Fluorescence Analysis

Subfield: Radiation

Field: Physics and Astronomy

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $3,830

OpenAlex ID: W2006574346

FWCI: 4.635

Cites: 17

Cited by: 31

Related to: 10