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discounted EARLY registration ends Dec 31, 2014
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discounted EARLY registration ends Dec 31, 2014
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discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 Enzyme: hydrogenase 3

Component of: formate hydrogenlyase complex

Subunit composition of hydrogenase 3 = [HycD][HycC][HycF][HycG][HycB][HycE]
         hydrogenase 3, membrane subunit = HycD (summary available)
         hydrogenase 3, membrane subunit = HycC (summary available)
         formate hydrogenlyase complex iron-sulfur protein = HycF (summary available)
         hydrogenase 3 and formate hydrogenlyase complex, HycG subunit = HycG (summary available)
         hydrogenase 3, Fe-S subunit = HycB (summary available)
         hydrogenase 3, large subunit = HycE (extended summary available)

Summary:
Microbial hydrogenases catalyse the reversible reduction of protons to molecular hydrogen. E. coli hydrogenase 3, encoded by the hyc genes (hycD, hycC, hycF, hycG, hycB and hycE), is a multisubunit enzyme that forms part of the formate hydrogenlyase (FHL) complex responsible for the fermentative or anaerobic oxidation of formic acid to carbon dioxide and molecular hydrogen [Peck57, Sawers85, Bohm90, Bagramyan03].

Hydrogenase 3 functions primarily in the production of H2 [Maeda07] and is important for H2 production at acidic pH [Bagramyan02, Mnatsakanyan04, Noguchi10]. Hydrogen uptake in a strain lacking hydrogenase 1 and hydrogenase 2 is further reduced by the incorporation of a hycE mutation, suggesting that hydrogenase 3 can also function in hydrogen uptake [Maeda07]. Hydrogenase 3 shows a high tolerance to product (H2) inhibition [McDowall14].

Hydrogenase 3 is a membrane associated H2 evolving respiratory [NiFe] hydrogenase. It contains the large (HycE) and small (HycG) subunits that are characteristic of 'standard' NiFe hydrogenases plus two additional hydrophilic subunits (HycB and HycF) and two inner membrane subunits (HycC and HycD). Fe-S prosthetic groups located in the hydrophilic part of the complex may form the electron transport pathway (reviews: [Vignais01, Hedderich05, Vignais08]). Isolation of FHL using affinity chromatography indicates the presence of a core complex containing HycE, HycB HycF HycG and FdhF which has formate hydrogenlyase activity in vitro; a larger complex containing the membrane assoicated subunits HyC and HycD is isolated in the presence of detergent [McDowall14]

Formate oxidation in an anaerobically grown fermenting E. coli strain lacking hydrogenase 1 and hydrogenase 2 enzymes generates membrane potential [Hakobyan05].

Sequence similarity between the genes encoding hydrogenase 3 and those encoding subunits that form the core of energy conserving NADH:quinone oxidoreductase (complex I) has been reported [Bohm90] and an evolutionary relationship between the two has been proposed [Hedderich04].

Strains with insertion mutations of genes within the hyc operon are defective for hydrogenase activity [Pecher83, Yerkes84].

Hydrogenase 3 is a nickel containing Fe-S protein [Rossmann94].

The hyc operon is regulated coordinately with the structural gene for formate dehydrogenase H. Expression is repressed by oxygen and by nitrate and induced by formate under fermentative growth conditions [Pecher83, Yerkes84]. Formate is an obligate inducer of the formate hydrogenlyase complex genes [Birkmann87].

E. coli K-12 contains three other hydrogenases: hydrogenase 1 and hydrogenase 2 (respiratory enzymes that function in H2 uptake) and hydrogenase 4 (less well characterised; possibly silent).

Reviews: [Sawers94, Lin91, Trchounian12]

Locations: inner membrane

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006113 - fermentation Inferred from experiment [Peck57]
GO:0015990 - electron transport coupled proton transport Inferred by computational analysis Inferred from experiment [Hakobyan05, Vignais08]
Molecular Function: GO:0008901 - ferredoxin hydrogenase activity Inferred from experiment [McDowall14]
GO:0033748 - hydrogenase (acceptor) activity Inferred from experiment [Bohm90, Pecher83]
Cellular Component: GO:0009375 - ferredoxin hydrogenase complex Inferred by computational analysis Inferred from experiment [McDowall14, Bohm90]
GO:0005887 - integral component of plasma membrane Inferred by computational analysis [Bohm90]

Credits:
Last-Curated ? 14-Sep-2014 by Mackie A , Macquarie University


Enzymatic reaction of: hydrogenase

a reduced hydrogenase 3 + 2 H+ <=> an oxidized hydrogenase 3 + H2

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

This reaction is reversible.


Subunit of: formate hydrogenlyase complex

Subunit composition of formate hydrogenlyase complex = [FdhF][(HycD)(HycC)(HycF)(HycG)(HycB)(HycE)]
         formate dehydrogenase H = FdhF (extended summary available)
         hydrogenase 3 = (HycD)(HycC)(HycF)(HycG)(HycB)(HycE) (extended summary available)
                 hydrogenase 3, membrane subunit = HycD (summary available)
                 hydrogenase 3, membrane subunit = HycC (summary available)
                 formate hydrogenlyase complex iron-sulfur protein = HycF (summary available)
                 hydrogenase 3 and formate hydrogenlyase complex, HycG subunit = HycG (summary available)
                 hydrogenase 3, Fe-S subunit = HycB (summary available)
                 hydrogenase 3, large subunit = HycE (extended summary available)


Enzymatic reaction of: formate hydrogenlyase complex

Synonyms: FHL-complex

formate + H+ <=> CO2 + H2

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: mixed acid fermentation


Subunit of hydrogenase 3: hydrogenase 3, membrane subunit

Synonyms: HevD, HycD, Ant-3, Ant-5

Gene: hycD Accession Numbers: EG10477 (EcoCyc), b2722, ECK2717

Locations: inner membrane

Sequence Length: 307 AAs

Molecular Weight: 33.029 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0005887 - integral component of plasma membrane Inferred by computational analysis [Bohm90]
GO:0009375 - ferredoxin hydrogenase complex Inferred by computational analysis [Bohm90]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
metabolism energy metabolism, carbon fermentation

Unification Links: EcoliWiki:b2722 , PR:PRO_000022956 , Protein Model Portal:P16430 , RefSeq:NP_417202 , SMR:P16430 , String:511145.b2722 , UniProt:P16430

Relationship Links: InterPro:IN-FAMILY:IPR001694 , InterPro:IN-FAMILY:IPR018086 , Panther:IN-FAMILY:PTHR11432 , Pfam:IN-FAMILY:PF00146 , Prosite:IN-FAMILY:PS00667 , Prosite:IN-FAMILY:PS00668

Summary:
The hycBCDEFG genes in E.coli K-12 encode the hydrogenase component (hydrogenase 3) of the formate hydrogenlyase complex. hycD encodes an extremely hydrophobic protein with 8 predicted transmembrane domains. The protein sequence has homology with one of the subunits of NADH:ubiquinone oxidoreductase of the respiratory chain [Bohm90, Sawers04].

Essentiality data for hycD knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of hydrogenase 3: hydrogenase 3, membrane subunit

Synonyms: HevC, HycC, Ant-2

Gene: hycC Accession Numbers: EG10476 (EcoCyc), b2723, ECK2718

Locations: inner membrane

Sequence Length: 608 AAs

Molecular Weight: 64.077 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0042773 - ATP synthesis coupled electron transport Inferred by computational analysis [GOA01a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred by computational analysis [GOA01a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0009375 - ferredoxin hydrogenase complex Inferred by computational analysis [Bohm90]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
metabolism energy metabolism, carbon fermentation

Unification Links: DIP:DIP-9973N , EcoliWiki:b2723 , Mint:MINT-1240211 , PR:PRO_000022955 , Protein Model Portal:P16429 , RefSeq:NP_417203 , SMR:P16429 , String:511145.b2723 , UniProt:P16429

Relationship Links: InterPro:IN-FAMILY:IPR001750 , InterPro:IN-FAMILY:IPR003918 , Pfam:IN-FAMILY:PF00361 , Prints:IN-FAMILY:PR01437

Summary:
The hycBCDEFG genes in E.coli K-12 encode the hydrogenase component (hydrogenase 3) of the formate hydrogenlyase complex. hycC encodes an extremely hydrophobic protein with 12 to 16 predicted transmembrane domains. The protein sequence has homology with one of the subunits of NADH:ubiquinone oxidoreductase of the respiratory chain [Bohm90, Sawers04].

Essentiality data for hycC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of hydrogenase 3: formate hydrogenlyase complex iron-sulfur protein

Synonyms: HevF, HycF

Gene: hycF Accession Numbers: EG10479 (EcoCyc), b2720, ECK2715

Locations: cytosol

Sequence Length: 180 AAs

Molecular Weight: 20.309 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred by computational analysis [UniProtGOA11a, Bohm90]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0009375 - ferredoxin hydrogenase complex Inferred by computational analysis [Bohm90]

MultiFun Terms: cell structure membrane
metabolism energy metabolism, carbon fermentation

Unification Links: EcoliWiki:b2720 , ModBase:P16432 , PR:PRO_000022958 , Pride:P16432 , Protein Model Portal:P16432 , RefSeq:NP_417200 , SMR:P16432 , String:511145.b2720 , Swiss-Model:P16432 , UniProt:P16432

Relationship Links: InterPro:IN-FAMILY:IPR001450 , InterPro:IN-FAMILY:IPR017896 , InterPro:IN-FAMILY:IPR017900 , Pfam:IN-FAMILY:PF00037 , Prosite:IN-FAMILY:PS00198 , Prosite:IN-FAMILY:PS51379

Summary:
The hycBCDEFG genes in E.coli K-12 encode the hydrogenase component (hydrogenase 3) of the formate hydrogenlyase complex. HycF is thought to be a 4Fe-4S ferredoxin type protein, an intermediate electron carrier protein [Bohm90, Lin91, Sauter92]. The protein resembles one of the subunits of NADH:ubiquinone oxidoreductase of the respiratory chain [Bohm90, Sawers04].

Essentiality data for hycF knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of hydrogenase 3: hydrogenase 3 and formate hydrogenlyase complex, HycG subunit

Synonyms: HevG, HycG

Gene: hycG Accession Numbers: EG10480 (EcoCyc), b2719, ECK2714

Locations: cytosol

Sequence Length: 255 AAs

Molecular Weight: 27.999 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Rajagopala12, Butland05]
GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred by computational analysis [GOA01a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0048038 - quinone binding Inferred by computational analysis [GOA01a]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0009375 - ferredoxin hydrogenase complex Inferred by computational analysis [Bohm90]

MultiFun Terms: metabolism energy metabolism, carbon fermentation

Unification Links: DIP:DIP-9977N , EcoliWiki:b2719 , Mint:MINT-1287919 , ModBase:P16433 , PR:PRO_000022959 , Protein Model Portal:P16433 , RefSeq:NP_417199 , SMR:P16433 , String:511145.b2719 , Swiss-Model:P16433 , UniProt:P16433

Relationship Links: InterPro:IN-FAMILY:IPR006137 , InterPro:IN-FAMILY:IPR006138 , InterPro:IN-FAMILY:IPR014406 , Panther:IN-FAMILY:PTHR11995 , Pfam:IN-FAMILY:PF01058 , Prosite:IN-FAMILY:PS01150

Summary:
The hycBCDEFG genes in E.coli K-12 encode the hydrogenase component (hydrogenase 3) of the formate hydrogenlyase complex. HycG has similarity to small subunits of hydrogenases [Sauter92] and resembles one of the subunits of NADH:ubiquinone oxidoreductase of the respiratory chain [Bohm90, Sawers04].

Essentiality data for hycG knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of hydrogenase 3: hydrogenase 3, Fe-S subunit

Synonyms: HevB, HycB

Gene: hycB Accession Numbers: EG10475 (EcoCyc), b2724, ECK2719

Locations: cytosol

Sequence Length: 203 AAs

Molecular Weight: 21.873 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred by computational analysis [UniProtGOA11a, Bohm90]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]
GO:0009375 - ferredoxin hydrogenase complex Inferred by computational analysis [Bohm90]

MultiFun Terms: metabolism energy metabolism, carbon fermentation

Unification Links: EcoliWiki:b2724 , ModBase:P0AAK1 , Pride:P0AAK1 , Protein Model Portal:P0AAK1 , RefSeq:NP_417204 , SMR:P0AAK1 , String:511145.b2724 , UniProt:P0AAK1

Relationship Links: InterPro:IN-FAMILY:IPR001450 , InterPro:IN-FAMILY:IPR017896 , InterPro:IN-FAMILY:IPR017900 , Pfam:IN-FAMILY:PF00037 , Pfam:IN-FAMILY:PF13187 , Prosite:IN-FAMILY:PS00198 , Prosite:IN-FAMILY:PS51379

Summary:
The hycBCDEFG genes in E.coli K-12 encode the hydrogenase component (hydrogenase 3) of the formate hydrogenlyase complex. HycB is believed to be a peptide of the [4Fe-4S] ferredoxin type, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase [Lin91, Sauter92, Trchounian00].

A hycB deletion mutant loses molecular hydrogen production and 2H+/K+ exchange abilities under anaerobic glucose-fermenting conditions. It is suggested that HycB is part of the formate-hydrogen lyase complex that interacts directly with the F0F1 ATPase complex and the TrkA system [Trchounian00].

Essentiality data for hycB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of hydrogenase 3: hydrogenase 3, large subunit

Synonyms: HevE, HycE, Ant-1

Gene: hycE Accession Numbers: EG10478 (EcoCyc), b2721, ECK2716

Locations: cytosol

Sequence Length: 569 AAs

Molecular Weight: 64.98 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Chung11, Chan11]
GO:0016151 - nickel cation binding Inferred from experiment Inferred by computational analysis [GOA01a, Rossmann94, Bohm90]
GO:0008137 - NADH dehydrogenase (ubiquinone) activity Inferred by computational analysis [GOA01a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016651 - oxidoreductase activity, acting on NAD(P)H Inferred by computational analysis [GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
GO:0048038 - quinone binding Inferred by computational analysis [GOA01a]
GO:0051287 - NAD binding Inferred by computational analysis [GOA01a]
GO:0051536 - iron-sulfur cluster binding Inferred by computational analysis [UniProtGOA11a]
GO:0051539 - 4 iron, 4 sulfur cluster binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol
GO:0009375 - ferredoxin hydrogenase complex Inferred by computational analysis [Bohm90]

MultiFun Terms: metabolism energy metabolism, carbon fermentation

Unification Links: DIP:DIP-9975N , EcoliWiki:b2721 , Mint:MINT-1223046 , ModBase:P16431 , PR:PRO_000022957 , Pride:P16431 , Protein Model Portal:P16431 , RefSeq:NP_417201 , SMR:P16431 , String:511145.b2721 , UniProt:P16431

Relationship Links: InterPro:IN-FAMILY:IPR001135 , InterPro:IN-FAMILY:IPR001268 , InterPro:IN-FAMILY:IPR001501 , InterPro:IN-FAMILY:IPR014029 , Pfam:IN-FAMILY:PF00329 , Pfam:IN-FAMILY:PF00346 , Pfam:IN-FAMILY:PF00374 , ProDom:IN-FAMILY:PD001581 , Prosite:IN-FAMILY:PS00535

Summary:
The hycBCDEFG genes in E.coli K-12 encode the hydrogenase component (hydrogenase 3) of the formate hydrogenlyase complex. HycE is the large subunit of hydrogenase 3 [Bohm90, Sauter92]. The protein has homolgy with one of the subunits of NADH:ubiquinone oxidoreductase of the respiratory chain [Bohm90, Sawers04].

Maturation of HycE requires incorporation of nickel followed by processing after the Arg537 residue by the HycI maturation endopeptidase [Rossmann94, Rossmann95, Binder96, Theodoratou00]. Maturation has been reconstituted in vitro and requires HypB, HypC, HypD, HypE, HypF, HycI and nickel, as it does in vivo [Maier96]. HypC interacts directly with pre-HycE and facilitates metal incorporation [Drapal98, Blokesch02]; mutational studies of conserved cysteine residues have led to a model for nickel incorporation [Magalon00]. After the incorporation of nickel, pre-HycE must dissociate from HypC to become a substrate for the HycI maturation endopeptidase [Magalon00a].

Protein engineering of HycE was able to produce a variant with 23-fold higher hydrogen production and nine-fold higher yield on formate compared to wildtype E. coli [Maeda08].

Essentiality data for hycE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bagramyan02: Bagramyan K, Mnatsakanyan N, Poladian A, Vassilian A, Trchounian A (2002). "The roles of hydrogenases 3 and 4, and the F0F1-ATPase, in H2 production by Escherichia coli at alkaline and acidic pH." FEBS Lett 516(1-3);172-8. PMID: 11959127

Bagramyan03: Bagramyan K, Trchounian A (2003). "Structural and functional features of formate hydrogen lyase, an enzyme of mixed-acid fermentation from Escherichia coli." Biochemistry (Mosc) 68(11);1159-70. PMID: 14640957

Binder96: Binder U, Maier T, Bock A (1996). "Nickel incorporation into hydrogenase 3 from Escherichia coli requires the precursor form of the large subunit." Arch Microbiol 165(1);69-72. PMID: 8639025

Birkmann87: Birkmann A, Zinoni F, Sawers G, Bock A (1987). "Factors affecting transcriptional regulation of the formate-hydrogen-lyase pathway of Escherichia coli." Arch Microbiol 1987;148(1);44-51. PMID: 2443100

Blokesch02: Blokesch M, Bock A (2002). "Maturation of [NiFe]-hydrogenases in Escherichia coli: the HypC cycle." J Mol Biol 324(2);287-96. PMID: 12441107

Bohm90: Bohm R, Sauter M, Bock A (1990). "Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components." Mol Microbiol 1990;4(2);231-43. PMID: 2187144

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Chan11: Chan Chung KC, Zamble DB (2011). "Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase." J Biol Chem 286(50);43081-90. PMID: 22016389

Chung11: Chung KC, Zamble DB (2011). "The Escherichia coli metal-binding chaperone SlyD interacts with the large subunit of [NiFe]-hydrogenase 3." FEBS Lett 585(2);291-4. PMID: 21185288

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Drapal98: Drapal N, Bock A (1998). "Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation." Biochemistry 37(9);2941-8. PMID: 9485446

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Hakobyan05: Hakobyan M, Sargsyan H, Bagramyan K (2005). "Proton translocation coupled to formate oxidation in anaerobically grown fermenting Escherichia coli." Biophys Chem 115(1);55-61. PMID: 15848284

Hedderich04: Hedderich R (2004). "Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I." J Bioenerg Biomembr 36(1);65-75. PMID: 15168611

Hedderich05: Hedderich R, Forzi L (2005). "Energy-converting [NiFe] hydrogenases: more than just H2 activation." J Mol Microbiol Biotechnol 10(2-4);92-104. PMID: 16645307

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Lin91: Lin EC, Iuchi S (1991). "Regulation of gene expression in fermentative and respiratory systems in Escherichia coli and related bacteria." Annu Rev Genet 1991;25;361-87. PMID: 1812811

Maeda07: Maeda T, Sanchez-Torres V, Wood TK (2007). "Escherichia coli hydrogenase 3 is a reversible enzyme possessing hydrogen uptake and synthesis activities." Appl Microbiol Biotechnol 76(5);1035-42. PMID: 17668201

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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