Related Experiment Video
Updated: Aug 30, 2026

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features
Published on: March 16, 2022
g-Strain, ENDOR, and structure of active centers of two-iron ferredoxins
W Richard Dunham1, Richard H Sands
1Department of Surgery, The University of Michigan Health System, Ann Arbor, MI 48109-0592, USA. wrdunham@umich.edu
Abstract:
Collaborative chemical and spectroscopic work from several laboratories resulted in a qualitative structure for the active center in the two-iron ferredoxins, with each iron being in a distorted tetrahedron of sulfur atoms (two acid-labile sulfurs bridging the two iron atoms and the other two from cysteine sulfurs). Subsequent X-ray data from other laboratories confirmed this structure. Detailed EPR spectral syntheses showed that there is a distribution of structures in any given protein (even in a single crystal) resulting in a distribution of the principal values of the g tensor, which may be described by a statistical distribution of still another tensor whose principal axes are, in general, not coincident with the principal-axis frame of the g tensor.
Related Concept Videos
Electron Transport Chain: Complex III and IV
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
The Photochemical Reaction Center
Electron Transport Chain Components
ATP Synthase: Structure

