Ultrafast Dynamics in Flavocytochrome C by Using Transient Absorption and Femtosecond Fluorescence Lifetime Spectroscopy
Year: 2025
Type: article
Abstract: High Resolution Image Download MS PowerPoint Slide Flavocytochrome c sulfide dehydrogenase (FCC) is an important enzyme of sulfur metabolism in sulfur-oxidizing bacteria, and its catalytic properties have been extensively studied. However, the ultrafast dynamics of FCC is not well understood. We present ultrafast transient absorption and fluorescence spectroscopy measurements to unravel the early events upon excitation of the heme and flavin chromophores embedded in the flavocytochrome c (FccAB) from the bacterium Thiocapsa roseopersicina . The fluorescence kinetics of FccAB suggests that the majority of the photoexcited species decay nonradiatively within the first few picoseconds. Transient absorption spectroscopy supports these findings by suggesting two major dynamic processes in FccAB, internal conversion occurring in about 400 fs and the vibrational cooling occurring in about 4 ps, mostly affecting the heme moiety.
Language: English
Subfield: Physical and Theoretical Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: hybrid
Awards: G12500569, G1390338878, G1402062977, G2244960170, G2695236191, G3463726684, G4131035492, Clarifying quantum limits in biomolecules by utilizing entangled photons generated from protein bound cofactor modeled on orange carotenoid protein, Time-resolved vibrational spectroscopy of proteins assisted by genetically encoded non-canonical amino acids, Objasnenie molekulárnych mechanizmov agregácie ľahkého reťazca IgG pri onkohematologických ochoreniach: od sérových proteínov po kinetické stabilizátory, G7694217703, G8088548421
OpenAlex ID: W4409258237