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Literature summary for 1.12.99.6 extracted from

  • Zhang, L.; Morello, G.; Carr, S.B.; Armstrong, F.A.
    Aerobic photocatalytic H2 production by a [NiFe] hydrogenase engineered to place a silver nanocluster in the electron relay (2020), J. Am. Chem. Soc., 142, 12699-12707 .
    View publication on PubMed
Search for more literature for 1.12.99.6

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information changing a tyrosine or threonine, located on the protein surface within 10 A of the distal [4Fe-4S] and medial [3Fe-4S] clusters, to cysteine, allows site-selective attachment of a silver nanocluster (AgNC), the reduced or photoexcited state of which is a powerful reductant. The AgNC provides a new additional redox site, capturing externally supplied electrons with sufficiently high energy to drive H2 production. Assemblies of Y227C (or T225C) with AgNCs/PMAA (PMAA = polymethyl acrylate templating several AgNC) are also electroactive for H2 production at a TiO2 electrode. A colloidal system for visible-light photo-H2 generation is made by building the hybrid enzyme into a heterostructure with TiO2 and graphitic carbon nitride (g-C3N4), the resulting scaffold promoting uptake of electrons excited at the AgNC. Eachhydrogenase produces 40 molecules of H2 per second and sustains 20% activity in air Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Escherichia coli 16020
-

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ACD8 hydrogenase-1 large chain
-
Escherichia coli K12 P0ACD8 hydrogenase-1 large chain
-

Oxidation Stability

Oxidation Stability Organism
the enzyme is O2-tolerant Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Subunits

Subunits Comment Organism
tetramer the membrane-extrinsic part of hydrogenase-1 is a dimer of heterodimers (alphabeta)2 Escherichia coli

Synonyms

Synonyms Comment Organism
Hyd-1
-
 Escherichia coli
hydrogenase-1
-
 Escherichia coli
[NiFe] hydrogenase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
Fe-S center the enzyme contains three FeS clusters: a distal [4Fe-4S]2+/1+ center, a medial [3Fe-4S]1+/0 center and a proximal [4Fe-3S]5+/4+ center Escherichia coli
[3Fe-4S]-center the enzyme contains three FeS clusters: a distal [4Fe-4S]2+/1+ center, a medial [3Fe-4S]1+/0 center and a proximal [4Fe-3S]5+/4+ center. The main reason for O2 tolerance is the presence of a special [4Fe-3S] cluster in the proximal position relative to the active site, which discharges a second electron when O2 attacks Escherichia coli
[4Fe-3S]-center the enzyme contains three FeS clusters: a distal [4Fe-4S]2+/1+ center, a medial [3Fe-4S]1+/0 center and a proximal [4Fe-3S]5+/4+ center Escherichia coli
[4Fe-4S]-center the enzyme contains three FeS clusters: a distal [4Fe-4S]2+/1+ center, a medial [3Fe-4S]1+/0 center and a proximal [4Fe-3S]5+/4+ center Escherichia coli