Enzymes
UniProtKB help_outline | 141 proteins |
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Reaction participants Show >> << Hide
- Name help_outline methanophenazine Identifier CHEBI:29118 (Beilstein: 8741237) help_outline Charge 0 Formula C37H50N2O InChIKeyhelp_outline VRHMBACMYZITGD-QAAQOENVSA-N SMILEShelp_outline CC(CCOc1ccc2nc3ccccc3nc2c1)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CCC=C(C)C 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
reduced coenzyme F420-(γ-Glu)n
Identifier
CHEBI:139511
Charge
-3
Formula
(C5H6NO3)n.C19H22N3O12P
Search links
Involved in 16 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:14378Polymer name: reduced coenzyme F420-(γ-L-Glu)(n)Polymerization index help_outline nFormula C19H22N3O12P(C5H6NO3)nCharge (-2)(-1)nMol File for the polymer
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- Name help_outline dihydromethanophenazine Identifier CHEBI:50375 Charge 0 Formula C37H52N2O InChIKeyhelp_outline LNCNNIYZOUNGMU-QAAQOENVSA-N SMILEShelp_outline CC(CCOc1ccc2Nc3ccccc3Nc2c1)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CCC=C(C)C 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,331 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
coenzyme F420-(γ-Glu)n
Identifier
CHEBI:133980
Charge
Formula
(C5H6NO3)n.C19H19N3O12P
Search links
Involved in 17 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:12939Polymer name: oxidized coenzyme F420-(γ-L-Glu)(n)Polymerization index help_outline nFormula C19H19N3O12P(C5H6NO3)nCharge (-3)(-1)nMol File for the polymer
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Cross-references
RHEA:54752 | RHEA:54753 | RHEA:54754 | RHEA:54755 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Goe1.
Abken H.J., Tietze M., Brodersen J., Baeumer S., Beifuss U., Deppenmeier U.
A hydrophobic, redox-active component with a molecular mass of 538 Da was isolated from lyophilized membranes of Methanosarcina mazei Gö1 by extraction with isooctane. After purification on a high-performance liquid chromatography column, the chemical structure was analyzed by mass spectroscopy an ... >> More
A hydrophobic, redox-active component with a molecular mass of 538 Da was isolated from lyophilized membranes of Methanosarcina mazei Gö1 by extraction with isooctane. After purification on a high-performance liquid chromatography column, the chemical structure was analyzed by mass spectroscopy and nuclear magnetic resonance studies. The component was called methanophenazine and represents a 2-hydroxyphenazine derivative which is connected via an ether bridge to a polyisoprenoid side chain. Since methanophenazine was almost insoluble in aqueous buffers, water-soluble phenazine derivatives were tested for their ability to interact with membrane-bound enzymes involved in electron transport and energy conservation. The purified F42OH2 dehydrogenase from M. mazei Gö1 showed highest activity with 2-hydroxyphenazine and 2-bromophenazine as electron acceptors when F420H2 was added. Phenazine-1-carboxylic acid and phenazine proved to be less effective. The Km values for 2-hydroxyphenazine and phenazine were 35 and 250 microM, respectively. 2-Hydroxyphenazine was also reduced by molecular hydrogen catalyzed by an F420-nonreactive hydrogenase which is present in washed membrane preparations. Furthermore, the membrane-bound heterodisulfide reductase was able to use reduced 2-hydroxyphenazine as an electron donor for the reduction of CoB-S-S-CoM. Considering all these results, it is reasonable to assume that methanophenazine plays an important role in vivo in membrane-bound electron transport of M. mazei Gö1. << Less
J. Bacteriol. 180:2027-2032(1998) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Methanophenazine: Structure, Total Synthesis, and Function of a New Cofactor from Methanogenic Archaea This work was supported by the Deutsche Forschungsgemeinschaft (Sonderforschungsbereich 416; grants De 488/6-1 and De 488/4-2) and the Fonds der Chemischen Industrie. We are grateful to Drs. J. Paust and H. Jaedicke (BASF AG, Ludwigshafen) and Dr. R. K. Muller (Hoffmann-La Roche Ltd., Basel) for generously providing chemicals.
Beifuss U., Tietze M., Baumer S., Deppenmeier U.
Angew Chem Int Ed Engl 39:2470-2472(2000) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Novel reactions involved in energy conservation by methanogenic archaea.
Deppenmeier U., Lienard T., Gottschalk G.
Methanogenic archaea of the order Methanosarcinales which utilize C(1) compounds such as methanol, methylamines or H(2)+CO(2), employ two novel membrane-bound electron transport systems generating an electrochemical proton gradient: the H(2):heterodisulfide oxidoreductase and the F(420)H(2):hetero ... >> More
Methanogenic archaea of the order Methanosarcinales which utilize C(1) compounds such as methanol, methylamines or H(2)+CO(2), employ two novel membrane-bound electron transport systems generating an electrochemical proton gradient: the H(2):heterodisulfide oxidoreductase and the F(420)H(2):heterodisulfide oxidoreductase. The systems are composed of the heterodisulfide reductase and either a membrane-bound hydrogenase or a F(420)H(2) dehydrogenase which is functionally homologous to the proton-translocating NADH dehydrogenase. Cytochromes and the novel electron carrier methanophenazine are also involved. In addition, the methyl-H(4)MPT:HS-CoM methyltransferase is bioenergetically relevant. The enzyme couples methyl group transfer with the translocation of sodium ions and seems to be present in all methanogens. The proton-translocating systems with the participation of cytochromes and methanophenazine have been found so far only in the Methanosarcinales. << Less
FEBS Lett. 457:291-297(1999) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Membrane-bound F420H2-dependent heterodisulfide reduction in methanococcus voltae.
Brodersen J., Gottschalk G., Deppenmeier U.
Washed membranes prepared from H2+CO2- or formate-grown cells of Methanococcus voltae catalyzed the oxidation of coenzyme F420H2 and the reduction of the heterodisulfide (CoB-S-S-CoM) of 2-mercaptoethanesulfonate and 7-mercaptoheptanoylthreonine phosphate, which is the terminal electron acceptor o ... >> More
Washed membranes prepared from H2+CO2- or formate-grown cells of Methanococcus voltae catalyzed the oxidation of coenzyme F420H2 and the reduction of the heterodisulfide (CoB-S-S-CoM) of 2-mercaptoethanesulfonate and 7-mercaptoheptanoylthreonine phosphate, which is the terminal electron acceptor of the methanogenic pathway. The reaction followed a 1:1 stoichiometry according to the equation: F420H2 + COB-S-S-CoM --> F420 + CoM-SH + CoB-SH. These findings indicate that the reaction depends on a membrane-bound F420H2-oxidizing enzyme and on the heterodisulfide reductase, which remains partly membrane-bound after cell lysis. To elucidate the nature of the F420H2-oxidizing protein, washed membranes were solubilized with detergent, and the enzyme was purified by sucrose density centrifugation, anion-exchange chromatography, and gel filtration. Several lines of evidence indicate that F420H2 oxidation is catalyzed by a membrane-associated F420-reducing hydrogenase. The purified protein catalyzed the H2-dependent reduction of methyl viologen and F420. The apparent molecular mass and the subunit composition (43, 37, and 27 kDa) are almost identical to those of the F420-reducing hydrogenase that has already been purified from Mc. voltae. Moreover, the N-terminus of the 37-kDa subunit is identical to the amino acid sequence deduced from the fruG gene of the operon encoding the selenium-containing F420-reducing hydrogenase from Mc. voltae. A distinct F420H2 dehydrogenase, which is present in methylotrophic methanogens, was not found in this organism. << Less