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Article Dans Une Revue European Journal of Inorganic Chemistry Année : 2011

Further Characterization of the [FeFe]-Hydrogenase Maturase HydG

Résumé

Recent work conducted in several laboratories has shown that the [FeFe]-hydrogenase maturase HydG synthesizes both CO and CN– from tyrosine. We have very recently found that although CN– synthesis does not need the [4Fe-4S] cluster found in the HydG C-terminal domain, CO synthesis does require it. We have also proposed that the +H2N·–CH2–CO2– radical is a precursor for these two active site ligands. Here, we have extended our characterization of both the wild-type enzyme and a ThiH-like HydG truncated mutant, with small angle X-ray scattering (SAXS) spectroscopy, homology modeling and functional studies.

Dates et versions

hal-01140285 , version 1 (08-04-2015)

Identifiants

Citer

Cécile Tron, Mickael V Cherrier, Patricia Amara, Lydie Martin, Martin Fauth, et al.. Further Characterization of the [FeFe]-Hydrogenase Maturase HydG. European Journal of Inorganic Chemistry, 2011, 2011 (7 SI), pp.1121-1127. ⟨10.1002/ejic.201001101⟩. ⟨hal-01140285⟩
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