R
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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Journal ArticleDOI
Profiling the outer membrane proteome during growth and development of the social bacterium Myxococcus xanthus by selective biotinylation and analyses of outer membrane vesicles.
Jörg Kahnt,Kryssia Aguiluz,Jürgen Koch,Anke Treuner-Lange,Anna Konovalova,Stuart Huntley,Michael Hoppert,Lotte Søgaard-Andersen,Reiner Hedderich +8 more
TL;DR: The data suggest that OMV have functions in predation and possibly in transfer of intercellular signaling molecules between cells, and suggest novel functions for these transporters.
Journal ArticleDOI
Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum.
TL;DR: Evidence is presented that in the autotrophic methanogen the four 2-oxoacid oxidoreductases have anabolic functions, Vor and Ior being involved in the biosynthesis of amino acids from fatty acids taken up from the growth medium, as shown by 14C-labelling studies.
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Heterodisulfide Reductase from Methanol‐Grown Cells of Methanosarcina Barkeri is not a Flavoenzyme
TL;DR: Results indicate that MbHdrD harbors the active site of heterodisulfide reduction and that a flavin is not involved in catalysis.
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The Heterodisulfide Reductase from Methanobacterium Thermoautotrophicum Contains Sequence Motifs Characteristic of pyridine‐Nucleotide‐Dependent Thioredoxin Reductases
TL;DR: Findings suggest that HdrA harbors the site of heterodisulfide reduction and that the catalytic mechanism of the enzyme is similar to that of pyridine-nucleotide-dependent thioredoxin reductase.
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The tungsten formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic for enzymes containing molybdopterin dinucleotide.
TL;DR: The primary structures of the four subunits Fwd ABCD of the tungsten enzyme from Methanobacterium thermoautotrophicum which were determined by cloning and sequencing the encoding genes fwdABCD were found to contain sequence motifs characteristic for molybdopterin-dinucleotide-containing enzymes indicating that this subunit harbors the active site.