| Title | Date | PubMed ID |
|---|
| Substitution of a conserved catalytic dyad into 2-KPCC causes loss of carboxylation activity. | 2016 Sep | 27447465 |
| Roles of the redox-active disulfide and histidine residues forming a catalytic dyad in reactions catalyzed by 2-ketopropyl coenzyme M oxidoreductase/carboxylase. | 2011 Sep | 21764916 |
| Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase. | 2011 Feb 4 | 21192936 |
| Mechanism of inhibition of aliphatic epoxide carboxylation by the coenzyme M analog 2-bromoethanesulfonate. | 2010 Aug 13 | 20551308 |
| Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase. | 2006 Jan 10 | 16388586 |
| Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase. | 2002 Oct 29 | 12390015 |
| Crystallization and preliminary X-ray analysis of a NADPH 2-ketopropyl-coenzyme M oxidoreductase/carboxylase. | 2001 Mar | 11223527 |
| Characterization of five catalytic activities associated with the NADPH:2-ketopropyl-coenzyme M [2-(2-ketopropylthio)ethanesulfonate] oxidoreductase/carboxylase of the Xanthobacter strain Py2 epoxide carboxylase system. | 2000 Feb 15 | 10684609 |
| A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. | 1999 Jul 20 | 10411892 |