Robert Dunleavy

Cache sensor domains of DUF3365/Tll0287 family bind covalent c-type heme through a CXXCH insertion; a signaling member behaves like an NO sensor, a stand-alone one like a redox protein.

This study elucidates the signaling mechanism of the E. coli Aer receptor by analyzing its redox-dependent structural changes and their impact on kinase domain conformation.

The paper identifies a bacterial NO-binding Cache_heme-HAMP receptor that interacts with a Ser/Thr kinase via conserved motifs, revealing a novel mechanism of NO signaling.

This paper uses ESR spectroscopy to study flavoprotein dynamics in bacterial cells, revealing structural insights and developing a genetically encoded probe for in-cell structural analysis.