Premium
Cofactor Regeneration of NAD + from NADH: Novel Water‐Forming NADH Oxidases
Author(s) -
Riebel Bettina R.,
Gibbs Phillip R.,
Wellborn William B.,
Bommarius Andreas S.
Publication year - 2002
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/1615-4169(200212)344:10<1156::aid-adsc1156>3.0.co;2-#
Subject(s) - nad+ kinase , chemistry , cofactor , biochemistry , enzyme , stereochemistry
Dehydrogenases with their superb enantioselectivity can be employed advantageously to prepare enantiomerically pure alcohols, hydroxy acids, and amino acids. For economic syntheses, however, the co‐substrate of dehydrogenases, the NAD(P)(H) cofactor, has to be regenerated. Whereas the problem of regenerating NADH from NAD + can be considered solved, the inverse problem of regenerating NAD + from NADH still awaits a definitive and practical solution. A possible solution is the oxidation of NADH to NAD + with concomitant reduction of oxygen catalyzed by NADH oxidase (E.C. 1.6.‐.‐) which can reduce O 2 either to undesirable H 2 O 2 or to innocuous H 2 O. We have found and cloned two novel genes from Borrelia burgdorferi and Lactobacillus sanfranciscensis with hitherto only machine‐annotated NADH oxidase function. We have overexpressed the corresponding proteins and could prove the annotated function to be correct. As demonstrated with a more sensitive assay than employed previously, the two novel NADH oxidases reduce O 2 to H 2 O.