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Literature summary for 1.12.1.4 extracted from

  • Berto, P.; Di Valentin, M.; Cendron, L.; Vallese, F.; Albertini, M.; Salvadori, E.; Giacometti, G.M.; Carbonera, D.; Costantini, P.
    The [4Fe-4S]-cluster coordination of [FeFe]-hydrogenase maturation protein HydF as revealed by EPR and HYSCORE spectroscopies (2012), Biochim. Biophys. Acta, 1817, 2149-2157.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermotoga neapolitana

Protein Variants

Protein Variants Comment Organism
C302S mutant displays a very weak electron paramagnetic resonance signal Thermotoga neapolitana
C353S mutant displays a very weak electron paramagnetic resonance signal Thermotoga neapolitana
C356S mutant displays a very weak electron paramagnetic resonance signal Thermotoga neapolitana
H304A similar to wild-type, mutant exhibits electron paramagnetic resonance signals characteristic of oxidized [3Fe-4S]+ cluster Thermotoga neapolitana
H352A similar to wild-type, mutant exhibits electron paramagnetic resonance signals characteristic of oxidized [3Fe-4S]+ cluster Thermotoga neapolitana

Organism

Organism UniProt Comment Textmining
Thermotoga neapolitana
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-
-

Synonyms

Synonyms Comment Organism
HydF
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Thermotoga neapolitana

Cofactor

Cofactor Comment Organism Structure
4Fe-4S-center displays electron paramagnetic resonance signals characteristic of oxidized [3Fe-4S]+ cluster. Cysteine residues C302, C353, and C356 are strictly required for the binding of the [4Fe-4S] cluster, whereas the fourth ligand of the coordination sphere can vary depending on the molecular environment created by local residues and/or experimental conditions Thermotoga neapolitana