Literature summary for 1.13.11.72 extracted from

Hirao, H.; Morokuma, K.
Ferric superoxide and ferric hydroxide are used in the catalytic mechanism of hydroxyethylphosphonate dioxygenase: a density functional theory investigation (2010), J. Am. Chem. Soc., 132, 17901-17909.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	the overall reaction pathway requires ferric superoxide and ferric hydroxide intermediates	Streptomyces viridochromogenes

Organism

Organism	UniProt	Comment	Textmining
Streptomyces viridochromogenes	Q5IW40	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	reaction starts with H-abstraction from the C2 position of 2-hydroxyethylphosphonate by a ferric superoxide-type intermediate. The resultant Fe(II)-OOH intermediate may follow either a hydroperoxylation or hydroxylation pathway, the former process being energetically more favorable. In the hydroperoxylation pathway, a ferrous-alkylhydroperoxo intermediate is formed, and then its O-O bond is homolytically cleaved to yield a complex of ferric hydroxide with a gem-diol radical. Subsequent C-C bond cleavage within the gem-diol leads to formation of an R-CH2 radical species and one of the two products, i.e., formic acid. The R-CH2 radical then intramolecularly forms a C-O bond with the ferric hydroxide to provide the other product, hydroxymethylphosphonate. The overall reaction pathway requires ferric superoxide and ferric hydroxide intermediates	Streptomyces viridochromogenes	?	-	?

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Release 2023.1 (January 2023)