Tuning C-Phycocyanin Photoactivity via pH-Mediated Assembly-Disassembly.

ABSTRACT: Environment-triggered protein conformational changes have garnered wide interest in both fundamental research, for deciphering in vivo acclimatory responses, and practical applications, for designing stimuli-responsive probes. Here, we propose a protein-chromophore regulatory mechanism that allows for manipulation of C-phycocyanin (C-PC) from Spirulina platensis by environmental pH and UV irradiation. Using small-angle X-ray scattering, a pH-mediated C-PC assembly-disassembly pathway, from monomers to nonamers, was unraveled. Such flexible protein matrices impart tunability to the embedded tetrapyrroles, whose photochemical behaviors were found to be modulated by protein assembly states. UV irradiation on C-PC triggers pH-dependent singlet oxygen (¹O₂) generati

SUBMITTER: Li Y 

PROVIDER: S-EPMC9131392 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature