Premium
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom