Why Nature Uses Radical SAM Enzymes so Widely: Electron Nuclear Double Resonance Studies of Lysine 2,3-Aminomutase Show the 5′-dAdo• "free Radical" Is Never Free

Journal of the American Chemical Society

Volumn 137, Issue 22, 2015, Pages 7111-7121

  Horitani, Masaki ^a   Byer, Amanda S ^b   Shisler, Krista A ^b   Chandra, Tilak ^b   Broderick, Joan B ^b   Hoffman, Brian M ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

^b MONTANA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; FREE RADICALS; MACHINERY; NUCLEAR MAGNETIC RESONANCE; REACTION KINETICS; VAN DER WAALS FORCES;

CATALYTIC CYCLES; ELECTRON NUCLEAR DOUBLE RESONANCE; ELECTRON NUCLEAR DOUBLE RESONANCE SPECTROSCOPIES; ENZYME SUPERFAMILIES; RADICAL REACTIONS; REDUCTIVE CLEAVAGE; S ADENOSYL L METHIONINES; VAN DER WAALS CONTACTS;

AMINO ACIDS;

ADENOSINE TRIPHOSPHATE; COBAMAMIDE; FREE RADICAL; LYSINE 2,3 AMINOMUTASE; RADICAL; S ADENOSYLMETHIONINE; ADENOSYLMETHIONINE HYDROLASE; HYDROLASE; LYSINE 2,3-AMINOMUTASE; METHIONINE; MUTASE;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CATALYSIS; CHEMICAL BOND; ELECTRON NUCLEAR DOUBLE RESONANCE; ENDPLATE POTENTIAL; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ISOMERIZATION; NITROGEN NUCLEAR MAGNETIC RESONANCE; PROTON NUCLEAR MAGNETIC RESONANCE; RADICAL REACTION; ELECTRON SPIN RESONANCE; METABOLISM; PROCEDURES;

ELECTRON SPIN RESONANCE SPECTROSCOPY; FREE RADICALS; HYDROLASES; INTRAMOLECULAR TRANSFERASES; METHIONINE;

EID: 84935860021     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/jacs.5b00498     Document Type: Article

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