Mechanism of NADH transfer among dehydrogenases
Författare
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.
Publiceringsår
1998
Språk
Engelska
Sidor
149-156
Publikation/Tidskrift/Serie
BBA - Protein Structure and Molecular Enzymology
Volym
1385
Issue
1
Länkar
- Publication in Lund University research portal
- 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
Dokumenttyp
Artikel i tidskrift
Förlag
Elsevier
Ämne
- Basic Medicine
Nyckelord
- Dehydrogenase
- Channelling
- Enzyme kinetics
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 0167-4838