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Reiner Hedderich

Researcher at Max Planck Society

Publications -  58
Citations -  7034

Reiner Hedderich is an academic researcher from Max Planck Society. The author has contributed to research in topics: Coenzyme M & Hydrogenase. The author has an hindex of 42, co-authored 58 publications receiving 6506 citations. Previous affiliations of Reiner Hedderich include University of Marburg & University of Illinois at Urbana–Champaign.

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Methanogenic archaea: ecologically relevant differences in energy conservation.

TL;DR: In methanogens with cytochromes, the first and last steps in methanogenesis from CO2 are coupled chemiosmotically, whereas in methenogens without cyto Chromes, these steps are energetically coupled by a cytoplasmic enzyme complex that mediates flavin-based electron bifurcation.
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The Genome of M. Acetivorans Reveals Extensive Metabolic and Physiological Diversity

James E. Galagan, +76 more
- 01 Apr 2002 - 
TL;DR: The complete genome sequence of an acetate-utilizing methanogen, Methanosarcina acetivorans C2A, is reported, which indicates the likelihood of undiscovered natural energy sources for methanogenesis, whereas the presence of single-subunit carbon monoxide dehydrogenases raises the possibility of nonmethanogenic growth.
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Anaerobic respiration with elemental sulfur and with disulfides

TL;DR: Anaerobic respiration with elemental sulfur/polysulfide or organic disulfides is performed by several bacteria and archaea, but has only been investigated in a few organisms in detail.
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The Genome Sequence of Methanosphaera stadtmanae Reveals Why This Human Intestinal Archaeon Is Restricted to Methanol and H2 for Methane Formation and ATP Synthesis

TL;DR: Four sets of mtaABC genes coding for methanol:coenzyme M methyltransferases were found in the genome of M. stadtmanae and exhibit homology to mta genes previously identified in Methanosarcina species, which explains why this archaeon is dependent on acetate for biosynthesis of cell components.
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The final step in methane formation. Investigations with highly purified methyl-CoM reductase (component C) from Methanobacterium thermoautotrophicum (strain Marburg).

TL;DR: In conclusion, methyl-CoM reductase was specific for H-S-HTP as electron donor and neither N-6-mercaptohexanoylthreonine phosphate (H- S-HxoTP) nor N-8-MERcaptooctanoyslthuronine phosphate(H-S)-OcoTP nor any other thiol compound could substitute for H -S- HTP.