A photochromic ATP analogue driving a motor protein with reversible light-controlled motility: controlling velocity and binding manner of a kinesin-microtubule system in an in vitro motility assay.

We synthesized two photochromic ATP analogues (ATP-Azos) featuring azobenzene derivatives tethered at the 2' position of the ribose ring. In the presence of the ATP-Azo tethering p-tert-butylazobenzene, we observed reversible photo-control of the motility, velocity and binding manner, of a kinesin-microtubule system in an in vitro motility assay.