1.12.99.6: hydrogenase (acceptor)
This is an abbreviated version!
For detailed information about hydrogenase (acceptor), go to the full flat file.
Word Map on EC 1.12.99.6
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1.12.99.6
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hydrogenases
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h-cluster
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nitrogenase
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reinhardtii
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chlamydomonas
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diiron
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ferredoxins
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dithiolate
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desulfovibrio
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hydf
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hupls
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subcluster
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maturase
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heterocystous
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nostoc
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organometallic
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eutropha
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acetobutylicum
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pasteurianum
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n2-fixing
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o2-tolerant
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diazotrophic
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photoproduction
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electrocatalytic
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electrocatalysts
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photobiological
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fhl
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mixed-valence
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gallinae
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hydrogen-producing
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biohydrogen
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overpotential
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nickel-containing
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cubane
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diphosphine
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sacrificial
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heterolytic
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oxygen-tolerant
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hydrogen-oxidizing
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h2-producing
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desulfuricans
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roseopersicina
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syntrophic
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h2-oxidizing
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photocatalytic
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f0f1-atpase
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h2ases
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thiocapsa
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industry
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brewing
- 1.12.99.6
- hydrogenases
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h-cluster
- nitrogenase
- reinhardtii
- chlamydomonas
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diiron
- ferredoxins
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dithiolate
- desulfovibrio
- hydf
-
hupls
-
subcluster
-
maturase
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heterocystous
- nostoc
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organometallic
- eutropha
- acetobutylicum
- pasteurianum
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n2-fixing
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o2-tolerant
-
diazotrophic
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photoproduction
-
electrocatalytic
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electrocatalysts
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photobiological
- fhl
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mixed-valence
- gallinae
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hydrogen-producing
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biohydrogen
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overpotential
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nickel-containing
- cubane
-
diphosphine
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sacrificial
-
heterolytic
-
oxygen-tolerant
-
hydrogen-oxidizing
-
h2-producing
- desulfuricans
- roseopersicina
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syntrophic
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h2-oxidizing
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photocatalytic
- f0f1-atpase
- h2ases
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thiocapsa
- industry
- brewing
Reaction
Synonyms
ECH, Ech hydrogenase, EchA, EchB, EchD, EchE, EchF, endo-hydrogenase, energy-converting hydrogenase, exo-hydrogenase, F420-reducing [NiFe] hydrogenase, factor420 hydrogenase, Fe-hydrogenase, Fe-only hydrogenase, ferredoxin hydrogenase, H2 producing hydrogenase [ambiguous], H2-sensing [NiFe] hydrogenase, Hfs, Hmd, HoxEFUYH type [NiFe] hydrogenase, HoxG, HupB, HupL, HupS, hupSLW, Hya, HyaA, HyaB, Hyb, HybA, HyC, HycE, Hyd X, Hyd-1, Hyd-2, Hyd-3, Hyd-4, HYD1, hydA, HydA1, HydA2, HydB, hydrogen dehydrogenase, hydrogen uptake hydrogenase, hydrogen-forming methylenetetrahydromethanopterin dehydrogenase, hydrogen-lyase, hydrogen-lyase [ambiguous], hydrogen:ferredoxin oxidoreductase, hydrogen:methylviologen oxidoreductase, hydrogenase (ferredoxin), hydrogenase 1, hydrogenase 2, hydrogenase 3, hydrogenase I (bidirectional), hydrogenase II, hydrogenase II (uptake), hydrogenase-1, hydrogenase-2, hydrogenase-Fe-S, hydrogenases Hyd-1, hydrogenases Hyd-2, hydrogenlyase [ambiguous], hyf, HyhL, HynSL, HynSL hydrogenase, Hyq, iron-sulfur-cluster-free hydrogenase, Mbh, membrane-bound [NiFe]-hydrogenase, methyl viologen-reducing hydrogenase, methylviologen hydrogenase, Ni-Fe hydrogenase, nickel-iron hydrogenase, NiFe hydrogenase, NiFe(Se) hydrogenase, NiFe-hydrogenase, NIFeSe-hydrogenase, regulatory hydrogenase, respiratory hydrogenase, SHI, uptake hydrogenase, uptake hydrogenase [ambiguous], uptake [NiFe] hydrogenase:, uptake [NiFe]-hydrogenase, [FeFe] hydrogenase, [FeFe]-H2ase, [FeFe]-hydrogenase, [FeFe]H2ase, [Fe] hydrogenase, [Fe]-hydA, [Fe]-hydrogenase, [Ni-Fe] hydrogenase, [NiFeSe]-hydrogenase, [NiFe] hydrogenase, [NiFe]-hydrogenase, [NiFe]-hydrogenase 2, [NiFe]-hydrogenase-2, [NiFe]H2ase, [NiFe]hydrogenase
ECTree
1.12.99.6 hydrogenase (acceptor)Advanced search results
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results (Engineering
Engineering on EC 1.12.99.6 - hydrogenase (acceptor)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
energy production
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use in photochemical energy conversion systems
C81S
theoretical 3D strucutural model. For the wild-type, the hydrogen bond of the network involving H82 and the bridging cysteines is formed with the sulfur atom of C78 whereas for the C81S mutant, it is formed with the bridging sulfur atom from C600. Calculations indicate a water molecule close to C81, which influences the IR spectra
F110L
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18% of wild-type H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation
I62V
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6% of wild-type H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation
I62V/F110L
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mutant enzyme shows no H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation
C81S
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theoretical 3D strucutural model. For the wild-type, the hydrogen bond of the network involving H82 and the bridging cysteines is formed with the sulfur atom of C78 whereas for the C81S mutant, it is formed with the bridging sulfur atom from C600. Calculations indicate a water molecule close to C81, which influences the IR spectra
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F110L
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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18% of wild-type H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation
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I62V
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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6% of wild-type H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation
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I62V/F110L
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
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mutant enzyme shows no H2 uptake activity. The loss of activity of the mutant protein originates from reversible oxidative inactivation
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D202V/K492
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variant epHycE70, has 11fold higher hydrogen production and 7fold higher hydrogen yield from formate compared to wild-type
D210N/I271F/K545R
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variant epHycE23-2, has 8fold higher hydrogen production and 4fold higher hydrogen yield from formate compared to wild-type
F297L/L327Q/E382K/L415M/A504T/D542N
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variant epHycE17, has 7fold higher hydrogen production and 4fold higher hydrogen yield from formate compared to wild-type
I333F/K554d
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variant epHycE39, has 7fold higher hydrogen production and 3fold higher hydrogen yield from formate compared to wild-type
Q32R/V112L/G245C/F409L
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variant epHycE21, has 15fold higher hydrogen production and 6fold higher hydrogen yield from formate compared to wild-type
S2P/E4G/M314V/T366S/V394D/S397C
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variant epHycE67, has 13fold higher hydrogen production and 5fold higher hydrogen yield from formate compared to wild-type
S2T/Y50F/I171T/A291V/T366S/V433L/M444I/L523Q
T366
Y464
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variant shufHycE1-9, has 23fold higher hydrogen production and 9fold higher hydrogen yield from formate compared to wild-type
F297L/L327Q/E382K/L415M/A504T/D542N
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variant epHycE17, has 7fold higher hydrogen production and 4fold higher hydrogen yield from formate compared to wild-type
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Q32R/V112L/G245C/F409L
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variant epHycE21, has 15fold higher hydrogen production and 6fold higher hydrogen yield from formate compared to wild-type
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S2T/Y50F/I171T/A291V/T366S/V433L/M444I/L523Q
C176A
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the Cys176 sulfur and unknown ligands of the iron complex of the wild-type enzyme are replaced by the dithiothreitol present in the crystallization solution
V74C
Solidesulfovibrio fructosivorans
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moderate increase in the Michaelis constant for H2. The mutant has the same oxidation activity as the wild-type whereas its maximal H2 production rate varies by 2 orders of magnitude
V74M
Solidesulfovibrio fructosivorans
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moderate increase in the Michaelis constant for H2, The mutant has the same oxidation activity as the wild-type whereas its maximal H2 production rate varies by 2 orders of magnitude. The ratio of maximal rates for oxidation over production ranges from 2.5 for the wild-type to 200 for the V74M mutant
A204F
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no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
D100N
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no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
D88N
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no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
E94Q
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no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
G125L
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no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
M203I
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no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
P129A
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no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
Y114F
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no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
Y127F
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no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
Y127H
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no difference in activity with 2,3-dimethyl1,4-naphthoquinone and benzyl viologen to wild-type
additional information
S2T/Y50F/I171T/A291V/T366S/V433L/M444I/L523Q
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shows a 17fold higher hydrogen-producing activity and 8fold higher hydrogen yield from formate than wild type HycE
S2T/Y50F/I171T/A291V/T366S/V433L/M444I/L523Q
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variant epHycE95, has 17fold higher hydrogen-producing activity and 8fold higher hydrogen yield from formate compared to wild-type
T366
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variant satHycE12T366, has 30fold higher hydrogen production compared to wild-type
T366
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variant satHycE19T366, has 27fold higher hydrogen production compared to wild-type
S2T/Y50F/I171T/A291V/T366S/V433L/M444I/L523Q
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shows a 17fold higher hydrogen-producing activity and 8fold higher hydrogen yield from formate than wild type HycE
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S2T/Y50F/I171T/A291V/T366S/V433L/M444I/L523Q
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variant epHycE95, has 17fold higher hydrogen-producing activity and 8fold higher hydrogen yield from formate compared to wild-type
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additional information
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site directed mutagenesis in conserved motifs of the subunit HoxH
additional information
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saturation mutagenesis at T366 of HycE leads to increased hydrogen production via a truncation at this position, 204 amino acids at the carboxy terminus may be deleted to increase hydrogen production by 30fold
additional information
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the uptake activity in mutant HD705/pBS(Kan), which is defective in hydrogenase 3, is 4.4fold lower than that in wild-type enzyme, the hydrogen uptake activity in the hydrogenase 1 and 2 double mutant (hyaB hybC) is reduced 2.7fold by addition of the hycE mutation (hyaB hybC hycE)
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
additional information
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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
additional information
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saturation mutagenesis at T366 of HycE leads to increased hydrogen production via a truncation at this position, 204 amino acids at the carboxy terminus may be deleted to increase hydrogen production by 30fold
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additional information
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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
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additional information
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deletion of the hfs gene results in a loss of detectable methyl viologen-linked hydrogenase activity. Strains with a deletion of the hfs genes exhibit a 95% reduction in hydrogen and acetic acid production. DELTAhfs strain produces primarily lactic acid in place of acetic acid, resulting in an ethanol yield relatively the same as the wild-type strain yield. A strain with hfs and ldh deletions exhibit an increased ethanol yield from consumed carbohydrates
