Mechanism and dynamics of photoswitchable flavoprotein charge-transfer complexes.

ABSTRACT: Because of their diverse uses in biological science and engineering, continued effort has been made to expand the pool of photoswitchable protein systems. A recent study demonstrated that in monomeric sarcosine oxidase (MSOX), photoexcitation of a charge-transfer (CT) complex formed by a flavin cofactor and a nonreactive ligand (e.g., methylthioacetate) induces the ligand to reversibly change conformation, with implications for the development of flavin-dependent fast photochromic proteins. However, the factors that control the underlying switching mechanism and dynamics remain largely unexplored. Herein, combining extensive protein mutagenesis, ultrafast laser spectroscopic measurements and classical and quantum computational approaches, we assess those factors in a range of protei

SUBMITTER: Zhuang B 

PROVIDER: S-EPMC11894434 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature