The role of NAD(P)H cofactor binding in alcohol dehydrogenase catalysis : = Die Rolle der Bindung des Cofaktors NAD(P)H für die Alkoholdehydrogenase-Katalyse
- Weitere Titel
-
Die Rolle der Bindung des Cofaktors NAD(P)H für die Alkoholdehydrogenase-Katalyse
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
Universität Freiburg, Dissertation, 2018
- Schlagwort
-
Alcohol dehydrogenase
Catalysis
Spectrum analysis
Circular dichroism
Alkoholdehydrogenasen
Zirkulardichroismus
Mutagenese
Enzymaktivität
- Ereignis
-
Veröffentlichung
- (wo)
-
Freiburg
- (wer)
-
Universität
- (wann)
-
2018
- Urheber
- Beteiligte Personen und Organisationen
- DOI
-
10.6094/UNIFR/16692
- URN
-
urn:nbn:de:bsz:25-freidok-166929
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:53 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
Entstanden
- 2018
Ähnliche Objekte (12)
Network-wide thermodynamic constraints shape NAD(P)H cofactor specificity of biochemical reactions
Interactions between HDL and NAD(P)H oxidase
1st International Conference on NAD(P)H Oxidases
Studies on NAD(P)H Dehydrogenase and its Role in Vitamin K Dependent Carboxylation
Application of WST-8 based colorimetric NAD(P)H detection for quantitative dehydrogenase assays
NAD(P)H cytochrome b5 oxidoreductase : role of cysteines
Endogenous mitochondrial NAD(P)H fluorescence can predict lifespan
Reaktivität von NAD(P)H gegenüber Oxidantien bei Bindung an Dehydrogenasen
NAD(P)H, a primary target of 1O2 in mitochondria of intact cells
A hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)H
Mouse Nudt13 is a Mitochondrial Nudix Hydrolase with NAD(P)H Pyrophosphohydrolase Activity
Quantification of NAD(P)H in cyanobacterial cells by a phenol extraction method
Network-wide thermodynamic constraints shape NAD(P)H cofactor specificity of biochemical reactions
Interactions between HDL and NAD(P)H oxidase
1st International Conference on NAD(P)H Oxidases
Studies on NAD(P)H Dehydrogenase and its Role in Vitamin K Dependent Carboxylation
Application of WST-8 based colorimetric NAD(P)H detection for quantitative dehydrogenase assays
NAD(P)H cytochrome b5 oxidoreductase : role of cysteines
Endogenous mitochondrial NAD(P)H fluorescence can predict lifespan
Reaktivität von NAD(P)H gegenüber Oxidantien bei Bindung an Dehydrogenasen
NAD(P)H, a primary target of 1O2 in mitochondria of intact cells
A hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)H
Mouse Nudt13 is a Mitochondrial Nudix Hydrolase with NAD(P)H Pyrophosphohydrolase Activity
Quantification of NAD(P)H in cyanobacterial cells by a phenol extraction method
Network-wide thermodynamic constraints shape NAD(P)H cofactor specificity of biochemical reactions
Interactions between HDL and NAD(P)H oxidase
1st International Conference on NAD(P)H Oxidases
Studies on NAD(P)H Dehydrogenase and its Role in Vitamin K Dependent Carboxylation
Application of WST-8 based colorimetric NAD(P)H detection for quantitative dehydrogenase assays
NAD(P)H cytochrome b5 oxidoreductase : role of cysteines
Endogenous mitochondrial NAD(P)H fluorescence can predict lifespan
Reaktivität von NAD(P)H gegenüber Oxidantien bei Bindung an Dehydrogenasen
NAD(P)H, a primary target of 1O2 in mitochondria of intact cells
A hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)H
Mouse Nudt13 is a Mitochondrial Nudix Hydrolase with NAD(P)H Pyrophosphohydrolase Activity