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Bacterial Methanogenesis Proceeds by a Radical Mechanism
Author(s) -
Buckel Wolfgang
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201304593
Subject(s) - chemistry , thiophosphate , intramolecular force , methylcobalamin , glycine , methane , cysteine , radical cyclization , photochemistry , medicinal chemistry , stereochemistry , enzyme , organic chemistry , biochemistry , amino acid , vitamin b12
The thiyl radical of cysteine 272 (C272) in the C‐P lyase adds to 5‐phosphoribose‐1‐methylphosphonate to give a covalently bound thiophosphonate radical. Reaction with glycine 32 (G32) of the enzyme yields methane, a glycyl radical, and thiophosphate (see scheme). Intramolecular attack of the 2‐OH group leads to 5‐phosphoribose‐1,2‐cyclic‐phosphate, whereas the glycyl radical oxidizes the liberated SH group back to the thiyl radical.