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Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea
- Anne-Kristin Kaster, J. Moll, K. Parey, R. Thauer
- Biology, ChemistryProceedings of the National Academy of Sciences
- 24 January 2011
It is reported here that the purified complex from Methanothermobacter marburgensis catalyzes the CoM-S- S-CoB-dependent reduction of ferredoxin with H2, indicating an electron bifurcation coupling mechanism.
NADP+ Reduction with Reduced Ferredoxin and NADP+ Reduction with NADH Are Coupled via an Electron-Bifurcating Enzyme Complex in Clostridium kluyveri
It was found that the purified iron-sulfur flavoprotein complex NfnAB couples the exergonic reduction of NADP+ with reduced ferredoxin (Fdred) and the endergonic Reduction of NADH with NADH in a reversible reaction.
Nickel, cobalt, and molybdenum requirement for growth of Methanobacterium thermoautotrophicum
Growth of Methanobacterium thermoautotrophicum on H2 and CO2 as sole energy and carbon sources was found to be dependent on Ni, Co, and Mo. At low concentrations of Ni (<100 nM), Co (<10 nM) and Mo…
Growth parameters (Ks, μmax, Ys) of Methanobacterium thermoautotrophicum
It is indicated that methane formation and growth are less tightly coupled at high concentrations of H2 or CO2 in the medium than at low concentrations.
The F₄₂₀-reducing [NiFe]-hydrogenase complex from Methanothermobacter marburgensis, the first X-ray structure of a group 3 family member.
Electron Bifurcation Involved in the Energy Metabolism of the Acetogenic Bacterium Moorella thermoacetica Growing on Glucose or H2 plus CO2
It is reported here that the 2 NADPH molecules required for CO(2) reduction to acetic acid are generated by the reduction of 2 NADP(+) molecules with 1 NADH and 1 Fd(red)(2-) catalyzed by the electron-bifurcating NADH-dependent reduced ferredoxin:NADP(+) oxidoreductase (NfnAB).
Sodium dependence of growth and methane formation in Methanobacterium thermoautotrophicum
The findings indicate that sodium has a specific function in the energy metabolism of this bacterium.
Five new EPR signals assigned to nickel in methyl-coenzyme M reductase from Methanobacterium thermoautotrophicum, strain Marburg
The crystal structure of an [Fe]-hydrogenase-substrate complex reveals the framework for H2 activation.
Structural basis of the hydride transfer mechanism in F(420)-dependent methylenetetrahydromethanopterin dehydrogenase.
The polypeptide scaffold does not reveal any significant conformational change upon binding of the bulky substrates but in turn changes the conformations of the substrate rings either to avoid clashes between certain ring atoms or to adjust the rings involved in hydride transfer for providing an optimal catalytic efficiency.