Figure 3.

Flavin reoxidation of cry1 in whole cell extracts. Isolated purified cry1 protein (10 μM) was photoreduced in PBS buffer at pH7.5, 5 mM DTT for 1 minute in white light (600 μmolm⁻²sec⁻¹) in the absence or presence (+ ATP) of 1mM ATP. Upon return to darkness, scans were taken at increasing time intervals and the absorption at 450 nm (peak absorption of oxidized flavin) monitored. % reoxidation represents the increase in A450 expressed as a percentage of the dark (pre-illumination) A450 peak value. Reoxidation of flavin in cry1 expressed in whole cell lysates was analyzed in the same way.