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Literature summary extracted from
- Direct electron transfer between the frhAGB-encoded hydrogenase and thioredoxin reductase in the nonmethanogenic archaeon Thermococcus onnurineus NA1 (2020), Appl. Environ. Microbiol., 86, e02630-19 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.12.98.1 | genes TON_1559 to TON_1561 or frhAGB gene cluster, DNA and amino acid sequence determination and analysis, recombinant expression as Strep-tagged proteins in Escherichia coli | Thermococcus onnurineus |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.12.98.1 | Fe2+ | the alpha-subunit (FrhA) contains a binuclear [Ni-Fe] center, the beta-subunit (FrhG) contains three [4Fe-4S] clusters, while the gamma-subunit (FrhB) has one [4Fe-4S] cluster | Thermococcus onnurineus |  |
| 1.12.98.1 | Ni2+ | the alpha-subunit (FrhA) contains a binuclear [Ni-Fe] center | Thermococcus onnurineus | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.9 | thioredoxin + NADP+ | Thermococcus onnurineus | - |
thioredoxin disulfide + NADPH + H+ | - |
r | |
| 1.8.1.9 | thioredoxin disulfide + H2 | Thermococcus onnurineus | - |
thioredoxin | - |
? | |
| 1.12.98.1 | H2 + oxidized coenzyme F420 | Thermococcus onnurineus | - |
reduced coenzyme F420 | - |
? | |
| 1.12.98.1 | H2 + thioredoxin | Thermococcus onnurineus | the frhAGB-encoded hydrogenase can transfer electrons derived from oxidation of H2 to a protein target by direct contact without the involvement of an electron carrier | reduced thioredoxin | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.1.9 | Thermococcus onnurineus | B6YUA8 | - |
- |
| 1.12.98.1 | Thermococcus onnurineus | B6YTV8 AND B6YTV9 AND B6YTW0 | Frh subunits A, B, and C | - |
| 1.12.98.1 | Thermococcus onnurineus | B6YTV8 AND B6YTV9 AND B6YTW0 AND | B6YTV8: alpha subunit, B6YTV9: gamma subunit, B6YTW0: beta subunit, B6YTW1: sulfur carrier protein FdhD | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.12.98.1 | recombinant Strep-tagged enzyme subunits from Escherichia coli by affinity chromatography | Thermococcus onnurineus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.9 | additional information | TrxR from Thermococcus onnurineus strain NA1 is known to catalyze the reduction of disulfide bonds of a Pdo protein by the electrons provided by NAD(P)H | Thermococcus onnurineus | ? | - |
- |
|
| 1.8.1.9 | thioredoxin + NADP+ | - |
Thermococcus onnurineus | thioredoxin disulfide + NADPH + H+ | - |
r | |
| 1.8.1.9 | thioredoxin disulfide + H2 | - |
Thermococcus onnurineus | thioredoxin | - |
? | |
| 1.12.98.1 | H2 + oxidized coenzyme F420 | - |
Thermococcus onnurineus | reduced coenzyme F420 | - |
? | |
| 1.12.98.1 | H2 + thioredoxin | the frhAGB-encoded hydrogenase can transfer electrons derived from oxidation of H2 to a protein target by direct contact without the involvement of an electron carrier | Thermococcus onnurineus | reduced thioredoxin | - |
? | |
| 1.12.98.1 | additional information | the endogenous frhAGB-encoded hydrogenase does not exhibit F420-reducing activity | Thermococcus onnurineus | ? | - |
- |
|
| 1.12.98.1 | oxidized methyl viologen + H2 | - |
Thermococcus onnurineus | reduced methyl viologen + H+ | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.12.98.1 | heterotrimer | alphabetagamma, 1 * 43000, alpha-subunit, + 1 * 30000, beta-subunit, + 1 * 25000, gamma-subunit, SDS-PAGE | Thermococcus onnurineus |
| 1.12.98.1 | More | enzyme peptide fingerprinting using matrix-assisted laser desorption ionization-time of flight tandem mass spectrometry (MALDI-TOF MS/MS) analysis | Thermococcus onnurineus |
| 1.12.98.1 | More | the Frh enzymes are encoded by the frhAGB genes and are heterotrimers composed of an alpha-subunit (FrhA) with a binuclear [Ni-Fe] center, a beta-subunit (FrhG) with three [4Fe-4S] clusters, and a gamma-subunit (FrhB) with one [4Fe-4S] cluster and one flavin adenine dinucleotide (FAD) as a prosthetic group | Thermococcus onnurineus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.8.1.9 | NADP-dependent thioredoxin reductase | - |
Thermococcus onnurineus |
| 1.8.1.9 | NTR | - |
Thermococcus onnurineus |
| 1.8.1.9 | thioredoxin reductase | - |
Thermococcus onnurineus |
| 1.8.1.9 | TON_1603 | - |
Thermococcus onnurineus |
| 1.8.1.9 | TrxR | - |
Thermococcus onnurineus |
| 1.12.98.1 | F420-reducing hydrogenase | - |
Thermococcus onnurineus |
| 1.12.98.1 | FrhABC | - |
Thermococcus onnurineus |
| 1.12.98.1 | frhAGB-encoded hydrogenase | - |
Thermococcus onnurineus |
| 1.12.98.1 | TON_1559 | - |
Thermococcus onnurineus |
| 1.12.98.1 | TON_1560 | - |
Thermococcus onnurineus |
| 1.12.98.1 | TON_1561 | - |
Thermococcus onnurineus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.9 | additional information | TrxR shows preference for NADPH over NADH | Thermococcus onnurineus | |
| 1.8.1.9 | NADPH | - |
Thermococcus onnurineus | |
| 1.12.98.1 | FAD | prosthetic group | Thermococcus onnurineus | |
| 1.12.98.1 | Fe-S center | the beta-subunit (FrhG) contains three [4Fe-4S] clusters, while the gamma-subunit (FrhB) has one [4Fe-4S] cluster | Thermococcus onnurineus | |
| 1.12.98.1 | additional information | the alpha-subunit (FrhA) contains a binuclear [Ni-Fe] center | Thermococcus onnurineus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.8.1.9 | metabolism | the TrxR/Pdo redox cascade can use H2 as the electron donor when the frhAGB-encoded hydrogenase mediates electron transfer. When FrhAGB is replaced with FrhAG, it also catalyzes the reduction of Pdo with slightly weaker activity. The specific activity of the FrhAG hydrogenase is 40% lower than that of the FrhAGB hydrogenase | Thermococcus onnurineus |
| 1.8.1.9 | physiological function | TrxR from the hyperthermophilic archaeon Thermococcus onnurineus strain NA1 is known to catalyze the reduction of disulfide bonds of a Pdo protein by the electrons provided by NAD(P)H. In Thermococcus onnurineus NA1, the frhAGB-encoded hydrogenase, a homologue of the F420-reducing hydrogenase of methanogens, interacts with thioredoxin reductase (TrxR). Electrons derived from H2 oxidation by the frhAGB-encoded hydrogenase are transferred to TrxR and reduced Pdo (protein disulfide oxidoreductase, UniProt ID B6YTB7), a redox partner of TrxR. Interaction and electron transfer are observed between TrxR and the heterodimeric hydrogenase complex (FrhAG) as well as the heterotrimeric complex (FrhAGB). Hydrogen-dependent reduction of TrxR is 7fold less efficient than when NADPH is the electron donor. TrxR can use H2 as an electron donor with the aid of the frhAGB-encoded hydrogenase as well as NADPH in Thermococcus onnurineus strain NA. The frhAGB-encoded hydrogenase can transfer electrons derived from oxidation of H2 to a protein target by direct contact without the involvement of an electron carrier, which is distinct from the mechanism of its homologue, F420-reducing hydrogenases of methanogens. The TrxR (TON_1603) of the hyperthermophilic archaeon Thermococcus onnurineus strain NA1 is a typical prokaryotic NADP-dependent thioredoxin reductase (NTR) with a preference for NADPH over NADH. The TrxR/Pdo redox couple is capable of reducing cystine to cysteine, which subsequently reduced dimethyl sulfoxide (DMSO) to dimethylsulfide (DMS). Because growth is enhanced by substituting DMSO for elemental sulfur (S0) as an electron sink for excess reducing power | Thermococcus onnurineus |
| 1.12.98.1 | evolution | the F420-binding motif of the frhB-encoded subunit is not well conserved | Thermococcus onnurineus |
| 1.12.98.1 | metabolism | electrons derived from H2 oxidation by the frhAGB-encoded hydrogenase are transferred to thioredoxin reductase (TrxR) and reduce Pdo, a redox partner of TrxR. Interaction and electron transfer are observed between TrxR and the heterodimeric hydrogenase complex (FrhAG) as well as the heterotrimeric complex (FrhAGB). Functionality of the frhAGB-encoded hydrogenase utilizing a protein as an electron acceptor | Thermococcus onnurineus |
| 1.12.98.1 | metabolism | in general, F420-reducing hydrogenases (Frh) are key enzymes in the hydrogenotrophic methanogenesis pathway in methanogens, providing reduced F420, which serves as an electron donor in the methylene-H4MPT dehydrogenase and the methylene-H4MPT reductase reactions. Redox cascade from the frhAGB-encoded hydrogenase to Pdo via TrxR | Thermococcus onnurineus |
| 1.12.98.1 | additional information | thioredoxin reductase (EC 1.8.1.9) TrxR might interact with the FrhA or FrhG subunit in the absence of the FrhB subunit | Thermococcus onnurineus |
| 1.12.98.1 | physiological function | in the hyperthermophilic archaeon Thermococcus onnurineus strain NA1, the frhAGB-encoded hydrogenase, a homologue of the F420-reducing hydrogenase of methanogens, interacts with thioredoxin reductase (TrxR EC 1.8.1.9). Electrons derived from H2 oxidation by the frhAGB-encoded hydrogenase are transferred to TrxR and reduced Pdo, a redox partner of TrxR. Interaction and electron transfer are observed between TrxR and the heterodimeric hydrogenase complex (FrhAG) as well as the heterotrimeric complex (FrhAGB). Hydrogen-dependent reduction of TrxR is 7fold less efficient than when NADPH is the electron donor. TrxR can use H2 as an electron donor with the aid of the frhAGB-encoded hydrogenase as well as NAD(P)H in Thermococcus onnurineus strain NA. The frhAGB-encoded hydrogenase can transfer electrons derived from oxidation of H2 to a protein target by direct contact without the involvement of an electron carrier, which is distinct from the mechanism of its homologues, F420-reducing hydrogenases of methanogens. F420-reducing hydrogenase (Frh) is a key enzyme in the hydrogenotrophic methanogenesis pathway in methanogens, providing reduced F420, which serves as an electron donor in the methylene-H4MPT dehydrogenase and the methylene-H4MPT reductase reactions | Thermococcus onnurineus |
| 1.12.98.1 | physiological function | key enzyme in the hydrogenotrophic methanogenesis pathway in methanogens, providing reduced F420, which serves as an electron donor in the methylene-tetrahydromethanopterin dehydrogenase and the methylene-tetrahydromethanopterin reductase reactions | Thermococcus onnurineus |
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