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Literature summary for 5.4.3.2 extracted from

  • Hinckley, G.T.; Frey, P.A.
    Cofactor dependence of reduction potentials for [4Fe-4S]2+/1+ in lysine 2,3-aminomutase (2006), Biochemistry, 45, 3219-3225.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Iron [4Fe-4S]2+/1+ couple shows midpoint reduction potentials of -430 mV in presence of S-adenosyl-L-methionine, -460 mV in presence of S-adenosyl-l-homocysteine, -497 mV in presence of 5’-(N-[(3S)-3-aminocarboxypropyl]-N-methylamino)-5’-deoxyadenosine. In presence of dithiothreitol, dihydrolipoate, or cysteine, midpoint potentials are -479, -516, and -484 mV, resp. Clostridium subterminale

Organism

Organism UniProt Comment Textmining
Clostridium subterminale
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Clostridium subterminale SB4
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