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Coenzyme binding at different ionization states of cytoplasmic and mitochondrial malate dehydrogenase

  • pH-titrations with NADH show two ionizable groups in mitochondrial and cytoplasmic malate dehydrogenase, the first with a pKa in the range 6.8 -8.3 for the mitochondrial and 6.4-7.8 for the cytoplasmic enzyme, the second with a lower limit at 10.2 resp. 11. Comparison with bis-(dihydronicotinamide)-dinucleotide and dihydronicotina-mide-ribosyl-P2-ribose-pyrophosphate instead of NADH indicates that the second alkaline ionization is caused by a residue placed near the adenine binding site of the active centre of the two isoenzymes. Binding studies with NADH and NAD+ give evidence for the participation of a group in the mitochondrial enzyme with pKa 6.8, deprotonation of which is necessary for detectable association of NAD+. In contrast the fixation of NAD+ to the cytoplasmic enzyme is independent of pH.

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Metadaten
Author:Klaus Schwerdtfeger, Christoph Woenckhaus, David M. Parker, John J. Holbrook
URN:urn:nbn:de:hebis:30:3-719371
DOI:https://doi.org/10.1515/znc-1982-5-632
ISSN:0939-5075
ISSN:1865-7125
Parent Title (German):Zeitschrift für Naturforschung, C
Publisher:Verlag der Zeitschrift für Naturforschung
Place of publication:Tübingen
Document Type:Article
Language:English
Date of Publication (online):2014/06/02
Year of first Publication:1982
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2024/02/05
Tag:Coenzyme Binding; Ionization State; Malate Dehydrogenases
Volume:37.1982
Issue:5-6
Page Number:3
First Page:547
Last Page:549
Institutes:Medizin
Biochemie, Chemie und Pharmazie / Biochemie und Chemie
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - Namensnennung-Nicht kommerziell-Keine Bearbeitung 3.0