Article
A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
Science (New York, N.Y.) - 29 Oct 2004
Frank René A W, Titman Christopher M, Pratap J Venkatesh, Luisi Ben F, Perham Richard N
Abstract excerpt
Thiamine diphosphate (ThDP) is used as a cofactor in many key metabolic enzymes. We present evidence that the ThDPs in the two active sites of the E1 (EC 1.2.4.1) component of the pyruvate dehydrogenase complex communicate over a distance of 20 angstroms by reversibly shuttling a proton through an acidic tunnel in the protein. This "proton wire" permits the co-factors to serve reciprocally as general acid/base in...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.