Photochemistry of Receptor-Bound Flavin Resolved in Living Human Cells by Infrared Spectroscopy.

ABSTRACT: In-cell experiments on proteins have revealed that the cellular environment can exert a considerable influence on protein mechanism and structure. Here, we introduce in-cell infrared difference spectroscopy (ICIRD) as a method to study soluble receptors in living human embryonic kidney cells by applying the attenuated total reflection approach. We demonstrate on the sensory domains of plant cryptochrome and aureochrome1a, a light, oxygen, or voltage (LOV) protein, that experiments can be performed using stable and transient transfection. Cells were cultivated and transfected on an internal reflection element directly inside the spectrometer, while their viability and growth were monitored in situ by infrared spectroscopy. Using ICIRD, we then resolved the photoreactions of oxidized

SUBMITTER: Goett-Zink L 

PROVIDER: S-EPMC11926855 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature