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carba Nicotinamide Adenine Dinucleotide Phosphate: Robust Cofactor for Redox Biocatalysis
Author(s) -
Zachos Ioannis,
Döring Manuel,
Tafertshofer Georg,
Simon Robert C.,
Sieber Volker
Publication year - 2021
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202017027
Subject(s) - cofactor , biocatalysis , nad+ kinase , nicotinamide adenine dinucleotide phosphate , nicotinamide adenine dinucleotide , chemistry , redox , niacinamide , nicotinamide , pyridinium , enzyme , stereochemistry , biochemistry , organic chemistry , reaction mechanism , catalysis , oxidase test
Abstract Here we report a new robust nicotinamide dinucleotide phosphate cofactor analog (carba‐NADP + ) and its acceptance by many enzymes in the class of oxidoreductases. Replacing one ribose oxygen with a methylene group of the natural NADP + was found to enhance stability dramatically. Decomposition experiments at moderate and high temperatures with the cofactors showed a drastic increase in half‐life time at elevated temperatures since it significantly disfavors hydrolysis of the pyridinium‐N−glycoside bond. Overall, more than 27 different oxidoreductases were successfully tested, and a thorough analytical characterization and comparison is given. The cofactor carba‐NADP + opens up the field of redox‐biocatalysis under harsh conditions.