Work

Does F1‐ATPase have a catalytic site that preferentially binds MgADP?

Year: 2006

Type: article

Abstract: During ATP synthesis, ATP synthase has to bind MgADP in the presence of an excess of MgATP. Thus, for efficient ATP synthesis it would be desirable if incoming substrate could be bound to a catalytic site with a preference for MgADP over MgATP. We tested three hypotheses predicting the existence of such a site. However, our results showed that, at least in absence of an electrochemical proton gradient, none of the three catalytic sites has a higher affinity for MgADP than for MgATP.

Source: FEBS Letters

DOI: 10.1016/j.febslet.2006.06.059

Authors: Hui Z. Mao, Wesley D. Gray, Joachim Weber

Institutions: Texas Tech University, Texas Tech University Health Sciences Center

Language: English

Topic: ATP Synthase and ATPases Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Awards: G4160636426, Catalytic mechanism of F1Fo-ATP synthase