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Salmonella enterica serovar Typhimurium has the ability to use molecular hydrogen as a respiratory electron donor. This is facilitated by three [NiFe]‐hydrogenases termed Hyd‐1, Hyd‐2 and Hyd‐5. Hyd‐1 and Hyd‐5 are homologous oxygen‐tolerant [NiFe]‐hydrogenases. A critical step in the biosynthesis of a [NiFe]‐hydrogenase is the proteolytic processing of the catalytic subunit. In this work, the role of the maturation protease encoded within the Hyd‐5 operon, HydD, was found to be partially complemented by the maturation protease encoded in the Hyd‐1 operon, HyaD. In addition, both maturation proteases were shown to form stable complexes, in vivo and in vitro, with the catalytic subunit of Hyd‐5. The protein‐protein interactions were not detectable in a strain that could not make the enzyme metallocofactor.
- Salmonella enterica
- anaerobic respiration
- bacterial hydrogen metabolism
- metalloenzyme biosynthesis
- protein‐protein interactions
FingerprintDive into the research topics of 'Identification of a stable complex between a [NiFe]‐hydrogenase catalytic subunit and its maturation protease'. Together they form a unique fingerprint.
- 1 Finished
Characterisation of Salmonella Enterica Hydrogenase-5 Biosynthesis for Developing Novel Anti-Infective Compounds (SalHyd5)
Albareda, M. & Sargent, F.
1/09/15 → 31/08/16