TY  - JOUR
A1  - Wönckhaus, Christoph Wilhelm
A1  - Jeck, Reinhard
T1  - Fluorometrische Untersuchungen über die Bildung von Enzym-Coenzym-Komplexen der Lactat-Dehydrogenase aus Schweineherz mit Coenzymbruchstücken und Coenzymmodellen
T2  - Zeitschrift für Naturforschung, B
N2  - Fluorescense spectra of lactate dehydrogenase * (E.C. 1.1.1.27) were investigated in the presence of the coenzyme fragments dihydronicotinamide mononucleotide and dihydronicotinamide-ribose-5'-pyrophospho- (P2) -5“-ribose. The reduced mononucleotide is enzymatically less active as a hydrogen donor. However, formation of a complex with the enzyme was not observed under the conditions used. All the other substances: dihydronicotinamide-ribose-5'-pyrophospho- (P2) -5“-ribose, dihydronicotinamide- benzimidazole-dinucleotide, dihydronicotinamide-3-desazapurine-dinucleotide and dihydronicotinamide-6-mercaptopurine-dinucleotide form more or less stable complexes with lactate dehydrogenase. The complexes do not markedly differ from the complex formed with the natural cofactor. In all cases spectra indicate change in conformation of the coenzyme by forming the coenzyme-enzyme-complex which has been proposed by VELICK 1 too. The cysteine residues of the lactate dehydrogenase are not essential for binding the coenzyme to the active center; this was shown with mercury blocked enzyme.
Y1  - 2014
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/74903
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-749033
SN  - 1865-7117
SN  - 0932-0776
VL  - 24
IS  - 11
SP  - 1436
EP  - 1441
PB  - Verlag der Zeitschrift für Naturforschung
CY  - Tübingen
ER  -