Mapping the cytochrome c553 interacting site using 1H and 15N NMR.
 

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