Karl Gruber
molekularbiologie.uni-graz.at
0000-0002-3485-9740
University of Graz
137 papers found
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A Biocatalytic Henry Reaction—The Hydroxynitrile Lyase fromHevea brasiliensis Also Catalyzes Nitroaldol Reactions
Vitamin B12: A Methyl Group without a Job?
Structure and Function of YcnD fromBacillus subtilis,a Flavin-Containing Oxidoreductase†,‡
Asymmetric biocatalytic hydrocyanation of pyrrole carboxaldehydes
B12-retro-Riboswitches: Constitutional Switching of B12Coenzymes Induced by Nucleotides
Homocoenzyme B12and Bishomocoenzyme B12: Covalent Structural Mimics for Homolyzed, Enzyme-Bound Coenzyme B12
Hydroxynitrile lyase catalysed synthesis of heterocyclic (R)- and (S)-cyanohydrins
2,6,9-Trioxabicyclo[3.3.1]nona-3,7-dien-4-oyl and tetraoxaadamantan-9-oyl functionalized aromatic di- and triamines: Synthesis, stereochemistry and complexation
The Cofactor of Tetrachloroethene Reductive Dehalogenase ofDehalospirillum multivorans Is Norpseudo-B12, a New Type of a Natural Corrinoid
Comprehensive Step-by-Step Engineering of an (R)-Hydroxynitrile Lyase for Large-Scale Asymmetric Synthesis
Biopolymers for biocatalysis: Structure and catalytic mechanism of hydroxynitrile lyases
Coenzyme B12 dependent glutamate mutase
The active site of hydroxynitrile lyase from Prunus amygdalus: Modeling studies provide new insights into the mechanism of cyanogenesis
Radical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl‐Radical Transfer in the Coenzyme B12 Dependent Enzyme Glutamate Mutase
The Hydroxynitrile Lyase from Almond
Metal Complexes of a Biconcave Porphyrin with D4-Structure—Versatile Chiral Shift Agents
Elucidation of the mode of substrate binding to hydroxynitrile lyase fromHevea brasiliensis
XAS spectroscopy reveals X-ray-induced photoreduction of free and protein-bound B12 cofactors
Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis
Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights
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