Flexibility of Thiamine Diphosphate Revealed by Kinetic Crystallographic Studies of the Reaction of Pyruvate-Ferredoxin Oxidoreductase with Pyruvate
Open Access
- 2 February 2006
- Vol. 14 (2) , 217-224
- https://doi.org/10.1016/j.str.2005.10.013
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- The Roles of Coenzyme A in the Pyruvate:Ferredoxin Oxidoreductase Reaction Mechanism: Rate Enhancement of Electron Transfer from a Radical Intermediate to an Iron−Sulfur ClusterBiochemistry, 2002
- The catalytic pathway of horseradish peroxidase at high resolutionNature, 2002
- Snapshot of a key intermediate in enzymatic thiamin catalysis: Crystal structure of the α-carbanion of (α,β-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiaeProceedings of the National Academy of Sciences, 2002
- Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin OxidoreductaseScience, 2001
- Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate.Nature Structural & Molecular Biology, 1999
- Crystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationActa Crystallographica Section D-Biological Crystallography, 1998
- Long bonds in cation radicals of vicinally difunctional moleculesJournal of the American Chemical Society, 1985
- A stable free radical intermediate in the reaction of 2‐oxoacid:ferredoxin oxidoreductases of Halobacterium halobiumFEBS Letters, 1980
- A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium.Proceedings of the National Academy of Sciences, 1966
- THE MECHANISM OF THIAMINE ACTION: PREDICTIONS FROM MODEL EXPERIMENTSAnnals of the New York Academy of Sciences, 1962