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Exploring the Mechanistic Diversity of Non‐Heme‐Iron Enzymes by Freeze‐Quench Mössbauer Spectroscopy
Author(s) -
Krebs Carsten,
Bollinger J. Martin
Publication year - 2016
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.30.1_supplement.112.3
Subject(s) - cofactor , heme , chemistry , enzyme , mössbauer spectroscopy , cleave , combinatorial chemistry , hemeprotein , stereochemistry , biochemistry , crystallography
Enzymes that activate dioxygen at a mononuclear or dinuclear non‐heme‐iron cofactor catalyze a wide variety of chemically difficult and biologically important oxidation reactions.(1–3) Our joint group is particularly interested in non‐heme‐iron enzymes that cleave aliphatic C‐H bonds. We study their reaction mechanisms by a combination of biochemical, kinetic, and spectroscopic methods.(4) This approach led to the identification of new cofactors,(5, 6) trapping and characterization of many reactive intermediates,(7, 8) and discovery of unexpected reactivities. The mechanistic diversity of these enzymes will be presented. Specifically, the role of 57 Fe‐Mössbauer spectroscopy in these studies will be highlighted.