Internal water molecules are considered to play a crucial role in the functional processes of
proton pump proteins. They may participate in hydrogen-bonding networks inside proteins …

Recent 3-D structures of several intermediates in the photocycle of bacteriorhodopsin (bR)
provide a detailed structural picture of this molecular proton pump in action. In this review …

The atomic structure of the light-driven ion pump bacteriorhodopsin and the surrounding
lipid matrix was determined by X-ray diffraction of crystals grown in cubic lipid phase. In the …

The plant blue light receptor, phot1, a member of the phototropin family (1), is a plasma
membrane-associated flavoprotein that contains two (∼ 110 amino acids) flavin-binding …

The promise of new architectures and more cost-effective miniaturization has prompted
interest in molecular and biomolecular electronics. Bioelectronics offers valuable near-term …

The transport of protons across membranes is an important process in cellular
bioenergetics. The light-driven proton pump bacteriorhodopsin is the best-characterized …

The proton transfer activity of the light-driven proton pump, bacteriorhodopsin (bR) in the
photochemical cycle might imply internal water molecules. The free energy of inserting water …

Channelrhodopsin-2 (ChR2) is a microbial type rhodopsin and a light-gated cation channel
that controls phototaxis in Chlamydomonas. We expressed ChR2 in COS-cells, purified it …

A wide variety of mechanisms are used to generate a proton-motive potential across cell
membranes, a function lying at the heart of bioenergetics. Bacteriorhodopsin, the simplest …

We have measured proton release into the medium after proton transfer from the retinal
Schiff base to Asp 85 in the photocycle and the C= O stretch bands of carboxylic acids in …