Literature summary for 1.13.11.20 extracted from

Pierce, B.S.; Gardner, J.D.; Bailey, L.J.; Brunold, T.C.; Fox, B.G.
Characterization of the nitrosyl adduct of substrate-bound mouse cysteine dioxygenase by electron paramagnetic resonance: electronic structure of the active site and mechanistic implications (2007), Biochemistry, 46, 8569-8578.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
electron paramagnetic study of substrate-O2 binding. Ordered binding of L-cysteine prior to NO and presumably O2. Upon addition of NO to cysteine dioxygenase in the presence of substrate L-cysteine, a low-spin(FeNO)7 signal with spin S of 1/2that accounts for 85% of the iron within the enzyme develops. Substitution of L-cysteine with isosteric substrate analogues cysteamine, 3-mercaptopropionic acid, and propane thiol does not produce any analogous signals.The unusual (FeNO)7, spin 1/2 electronic configuration adopted by the substrate-bound iron-nitrosyl cysteine dioxygenase is a result of the bidentate thiol/amine coordination of L-cysteine in the NO-bound active site	Mus musculus

Crystallization (Comment)

Organism

electron paramagnetic study of substrate-O2 binding. Ordered binding of L-cysteine prior to NO and presumably O2. Upon addition of NO to cysteine dioxygenase in the presence of substrate L-cysteine, a low-spin(FeNO)7 signal with spin S of 1/2that accounts for 85% of the iron within the enzyme develops. Substitution of L-cysteine with isosteric substrate analogues cysteamine, 3-mercaptopropionic acid, and propane thiol does not produce any analogous signals.The unusual (FeNO)7, spin 1/2 electronic configuration adopted by the substrate-bound iron-nitrosyl cysteine dioxygenase is a result of the bidentate thiol/amine coordination of L-cysteine in the NO-bound active site

Mus musculus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	non-heme iron	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	P60334	-	-

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Release 2023.1 (January 2023)