New insights from spectroscopy into the structure/function relationships of lipoxygenases.
Spectroscopic properties of the redox-active iron in the active site of plant and mammalian lipoxygenases can now be combined with recent crystal structure determinations to obtain new insights into lipoxygenase reaction mechanisms.
Solomon
E I
EI
Department of Chemistry, Stanford University, Standford, CA 94805, USA. solomon@chem.stanford.edu
Zhou
J
J
Neese
F
F
Pavel
E G
EG
D018360:Crystallography, X-Ray; D007501:Iron / Q000378:metabolism; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism*; D008084:Lipoxygenase / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013025:Glycine max / Q000201:enzymology; D013053:Spectrophotometry; D013329:Structure-Activity Relationship
D007527:Isoenzymes; D007501:Iron; D008084:Lipoxygenase