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ELDOR Spectroscopy Reveals that Energy Landscapes in Human Methionine Synthase Reductase are Extensively Remodelled Following Ligand and Partner Protein Binding
Author(s) -
Rigby Stephen E. J.,
Lou Xiaodong,
Toogood Helen S.,
Wolthers Kirsten R.,
Scrutton Nigel S.
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000630
Subject(s) - chemistry , methionine synthase , electron transfer , methionine , cofactor , ligand (biochemistry) , flavin group , biophysics , biochemistry , enzyme , biology , amino acid , photochemistry , receptor
ELDOR roadmap: ELDOR spectroscopy gives access to the energy landscape of an electron transfer protein. In human methionine synthase reductase (MSR) this landscape is rugged and is remodelled through effector ligand and protein binding. The mobility of flavin‐binding domains suggests that large‐scale motion underpins electron transfer across multiple redox cofactors in the MSR–methionine synthase protein complex (see figure).