The way bacteriorhodopsin generates a proton gradient in Archaea is through a proton pump. The proton pump relies on proton carriers to drive protons from the side of the membrane with a low H concentration to the side of the membrane with a high H concentration. In bacteriorhodopsin, the proton pump is activated by absorption of photons of 568nm wavelength, which leads to isomerization of the Schiff base (SB) in retinal forming the K state. This moves SB away from Asp85 and Asp212, causing H transfer from the SB to Asp85 forming the M1 state. The protein then shifts to the M2 state by separating Glu204 from Glu194 which releases a proton from Glu204 into the external medium. The SB is reprotonated by Asp96 which forms the N state. It is important that the second proton comes from Asp96 since its deprotonated state is unstable and rapidly reprotonated with a proton from the cytosol. The protonation of Asp85 and Asp96 causes re-isomerization of the SB, forming the O state. Finally, bacteriorhodopsin returns to its resting state when Asp85 releases its proton to Glu204.