Mapping the cytochrome c553 interacting site using 1H and 15N NMR.
Related Articles Mapping the cytochrome c553 interacting site using 1H and 15N NMR.
FEBS Lett. 1999 Oct 22;460(1):77-80
Authors: Morelli X, Guerlesquin F
Cytochrome c553 is the electron transfer partner of formate dehydrogenase and of [Fel-hydrogenase, two metalloenzymes essential in the metabolism of sulfate reducing bacteria. These two enzymes contain a 'ferredoxin-like' domain which presents 30% identity with Desulfovibrio desulfuricans Norway ferredoxin 1. This was chosen as a model for the 'ferredoxin-like' domain involved in the electron transfer reaction with cytochrome c553. ID NMR titration of complex formation gave us the stoichiometry (1:1) and the dissociation constant of the complex (Kd approximately 3x10(-6) M). 2D heteronuclear NMR experiments were performed to analyze the 1H and 15N chemical shift variations that are induced by the protein-protein recognition. This is the first mapping of the interaction site on a c-type cytochrome, using heteronuclear NMR.
PMID: 10571064 [PubMed - indexed for MEDLINE]
Source:
PubMed