Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase
- Research Organization:
- SLAC National Accelerator Lab., Menlo Park, CA (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC)
- DOE Contract Number:
- AC02-76SF00515
- OSTI ID:
- 1092133
- Report Number(s):
- SLAC-REPRINT-2013-589
- Journal Information:
- FEBS Letters, Vol. 585, Issue 3; ISSN 0014-5793
- Publisher:
- Federation of European Biochemical Societies
- Country of Publication:
- United States
- Language:
- English
Similar Records
Structural Basis for CO2 Fixation by a Novel Member of the Disulfide Oxidoreductase Family of Enzymes, 2-Ketopropyl-Coenzyme M Oxidoreductase/Carboxylase
Mechanistic Implications of the Structure of the Mixed-Disulfide Intermediate of the Disulfide Oxidoreductase, 2-Ketopropyl-Coenzyme Moxidoreductase/Carboxylase
A catalytic dyad modulates conformational change in the CO2-fixing flavoenzyme 2-ketopropyl coenzyme M oxidoreductase/carboxylase
Journal Article
·
Tue Jan 01 00:00:00 EST 2002
· Biochemistry
·
OSTI ID:1092133
Mechanistic Implications of the Structure of the Mixed-Disulfide Intermediate of the Disulfide Oxidoreductase, 2-Ketopropyl-Coenzyme Moxidoreductase/Carboxylase
Journal Article
·
Fri Jun 30 00:00:00 EDT 2006
· Biochemistry
·
OSTI ID:1092133
+2 more
A catalytic dyad modulates conformational change in the CO2-fixing flavoenzyme 2-ketopropyl coenzyme M oxidoreductase/carboxylase
Journal Article
·
Thu Mar 31 00:00:00 EDT 2022
· Journal of Biological Chemistry
·
OSTI ID:1092133
+2 more