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ProteomicsStructural analysis of the HypCD apo- and holoproteins by crosslinking mass spectrometry
[NiFe]-hydrogenases catalyse the reversible splitting of hydrogen. The catalytic metal centre (NiFe(CN)2CO) is unique in biology, and assembled by an intricate protein machinery, in a process that is still being explored. We hypothesised a structural, ATP-dependent, mechanistic explanation for the a...
ORGANISM(S): Escherichia coli 
2024-10-28 | PXD051661 | Pride
[nife]-hydrogenase assembly Photocrosslinking ms Hypcd 
UnknownElectron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly.
Not available
S-EPMC8454700 | biostudies-literature
UnknownATP-Triggered Fe(CN)2CO Synthon Transfer from the Maturase HypCD to the Active Site of Apo-[NiFe]-Hydrogenase.
Not available
S-EPMC11565642 | biostudies-literature
UnknownA conserved aspartate residue in [4Fe-4S]-containing HypD is required for [NiFe]-cofactor biosynthesis and for efficient interaction of the HypCD scaffold complex with HypE.
Not available
S-EPMC12130793 | biostudies-literature
UnknownEvidence the Isc iron-sulfur cluster biogenesis machinery is the source of iron for [NiFe]-cofactor biosynthesis in Escherichia coli.
Not available
S-EPMC10847431 | biostudies-literature
UnknownA redox-active HybG-HypD scaffold complex is required for optimal ATPase activity during [NiFe]-hydrogenase maturation in Escherichia coli.
Not available
S-EPMC9900092 | biostudies-literature
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