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Literature summary for 1.12.1.3 extracted from

  • Nouailler, M.; Morelli, X.; Bornet, O.; Chetrit, B.; Dermoun, Z.; Guerlesquin, F.
    Solution structure of HndAc: a thioredoxin-like domain involved in the NADP-reducing hydrogenase complex (2006), Protein Sci., 15, 1369-1378.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression of C-terminal domain of subunit HndA and N-terminal domain of subunit HndD in Escherichia coli Solidesulfovibrio fructosivorans

Metals/Ions

Metals/Ions Comment Organism Structure
Fe the HndA subunit belongs to the [2Fe-2S] ferredoxin family. HndB is a FeS subunit Solidesulfovibrio fructosivorans

Organism

Organism UniProt Comment Textmining
Solidesulfovibrio fructosivorans
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Purification (Commentary)

Purification (Comment) Organism
C-terminal domain of subunit HndA and N-terminal domain of subunit HndD recombinantly expressed in Escherichia coli Solidesulfovibrio fructosivorans

Subunits

Subunits Comment Organism
tetramer the HndC subunit (52 kDa) corresponds to the NADP-reducing unit, and the HndD subunit (63.5 kDa) is homologous to Clostridium pasteurianum hydrogenase. The role of HndA and HndB subunits (18.8 kDa and 13.8 kDa, respectively) in the complex remains unknown. HndAc and HndB can form a heterodimeric intermediate in the electron transfer between the hydrogenase (HndD) active site and the NADP reduction site in HndC Solidesulfovibrio fructosivorans