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Published February 2, 2007 | Supplemental Material + Accepted Version
Journal Article Open

Assignment of Individual Metal Redox States in a Metalloprotein by Crystallographic Refinement at Multiple X-ray Wavelengths

Abstract

A method is presented to derive anomalous scattering contributions for individual atoms within a protein crystal by collecting several sets of diffraction data at energies spread along an X-ray absorption edge of the element in question. The method has been applied to a [2Fe:2S] ferredoxin model system with localized charges in the reduced state of the iron−sulfur cluster. The analysis shows that upon reduction the electron resides at the iron atom closer to the protein surface. The technique should be sufficiently sensitive for more complex clusters with noninteger redox states and is generally applicable given that crystals are available.

Additional Information

© 2007 American Chemical Society Received October 23, 2006 Diffraction data were collected at SSRL, Stanford, and EMBL/DESY, Hamburg, Germany. This work was supported in part by EMBO YIP (O.E.), DFG (O.E., S.L.A.A.), CNRS and UJF (J.M.), and by NIH Grant GM45162 (D.C.R.).

Attached Files

Accepted Version - nihms61980.pdf

Supplemental Material - ja067562osi20061023_065527.pdf

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Created:
August 19, 2023
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October 18, 2023