Crystal structures and atomic model of NADPH oxidase

• DOI: 10.1073/pnas.1702293114
• Publication Date: 2017-06-13T00:50:28Z
• Authors: Francesca Magnani; Simone Nenci; Elisa Millana Fan...; Marta Ceccon; Elvira Romero; Marco W. Fraaije; Andrea Mattevi
• Keywords: Compartment (ship)

Significance Reactive oxygen species (ROS) are far from being only an inevitable byproduct of respiration. They instead actively generated by NADPH oxidases (NOXs), a family highly regulated enzymes that underpin complex functions in the control cell proliferation and antibacterial defense. By investigating individual catalytic domains, we elucidate core NOX 3D structure. An array cofactors is spatially organized to transfer reducing electrons intracellular milieu ROS-generating site, exposed outer side membrane. This redox chain finely tuned structural elements cooperate binding, thereby preventing noxious spills ROS. Our findings indicate avenues for pharmacological manipulation activity.