Article
Characterization of the hydrogen-deuterium exchange activities of the energy-transducing HupSL hydrogenase and H(2)-signaling HupUV hydrogenase in Rhodobacter capsulatus.
Journal of bacteriology - 1 Nov 2000
Vignais P M, Dimon B, Zorin N A, Tomiyama M, Colbeau A
Abstract excerpt
Rhodobacter capsulatus synthesizes two homologous protein complexes capable of activating molecular H(2), a membrane-bound [NiFe] hydrogenase (HupSL) linked to the respiratory chain, and an H(2) sensor encoded by the hupUV genes. The activities of hydrogen-deuterium (H-D) exchange catalyzed by the hupSL-encoded and the hupUV-encoded enzymes in the presence of D(2) and H(2)O were studied comparatively. Whereas...
Topics
- Acetylene
- Bacterial Proteins
- DNA-Binding Proteins
- Deuterium
- Hydrogen
- Hydrogen-Ion Concentration
- Kinetics
- Membrane Proteins
- Multigene Family
- Mutation
- Oxidoreductases
- Oxygen
- Proteins
- Rhodobacter capsulatus