Mechanism of NADH transfer among dehydrogenases

Summary, in English

Steady-state and transient-state kinetic experiments have been performed to test the proposal that there is a direct (channelled) transfer of NADH from one dehydrogenase to another if the two enzymes exhibit distinct chiral coenzyme specificity (A-side vs. B-side). The results lend no support to this proposal, but are fully consistent with a free-diffusion mechanism of NADH transfer irrespective of the chiral specificity of the enzymes.

• Author: Wilma Martinez Arias; Henrik Pettersson; Gösta Pettersson
• Department/s: Department of Experimental Medical Science; Biochemistry and Structural Biology
• Publishing year: 1998
• Language: English
• Pages: 149-156
• Publication/Series: BBA - Protein Structure and Molecular Enzymology
• Volume: 1385
• Issue: 1
• Links: http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T21-3T1BX85-J&_user=745831&_coverDate=06%2F11%2F1998&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_acct=C000041498&_version=1&_urlVersion=0&_userid=745831&md5=24580464b263977f32200263048dd1ff&searchtype=a; http://dx.doi.org/10.1016/S0167-4838(98)00035-1
• Document type: Journal article
• Publisher: Elsevier
• Topic: Basic Medicine
• Keywords: Dehydrogenase; Channelling; Enzyme kinetics
• Status: Published
• ISBN/ISSN/Other: ISSN: 0167-4838