Protein-Driven Electron-Transfer Process in a Fatty Acid Photodecarboxylase DOI Creative Commons
Giacomo Londi, Giacomo Salvadori, Patrizia Mazzeo

и другие.

JACS Au, Год журнала: 2024, Номер unknown

Опубликована: Дек. 17, 2024

Naturally occurring photoenzymes are rare in nature, but among them, fatty acid photodecarboxylases derived from Chlorella variabilis (CvFAPs) have emerged as promising photobiocatalysts capable of performing the redox-neutral, light-induced decarboxylation free acids (FAs) into C1-shortened n-alka(e)nes. Using a hybrid QM/MM approach combined with polarizable embedding scheme, we identify structural changes active site and determine energetic landscape forward electron transfer (fET) FA substrate to excited flavin adenine dinucleotide. We obtain charge-transfer diradical structure where water molecule rearranges spontaneously form H-bond interaction flavin, while FA's carboxylate group twists migrates away it. Together, these modifications provide driving force necessary for fET proceed downhill direction. Moreover, by examining R451K mutant is farther core, show that marked reduction electronic coupling counterbalanced an increased force, resulting lifetime similar WT, thereby suggesting resilience process this mutation. Finally, through molecular dynamic simulations, reveal that, following fET, radical occurs within tens picoseconds, overcoming energy barrier ∼0.1 eV. Overall, providing atomistic characterization photoactivation CvFAP, work can be used future protein engineering.

Язык: Английский

Decomplexation of cu(II)-EDTA by liquid-phase plasma: Enhanced performance by inducing self-catalytic Fenton reaction DOI
Ji Yeon Kim, Ui-Jun Kim, Seunghyo Lee

и другие.

Journal of Water Process Engineering, Год журнала: 2025, Номер 71, С. 107356 - 107356

Опубликована: Фев. 25, 2025

Язык: Английский

Процитировано

0
Mechanistic investigation of repurposed photoenzymes with new-to-nature reactivity DOI
Zhengyi Zhang, Mao‐Lin Li, Huimin Zhao

и другие.

Current Opinion in Green and Sustainable Chemistry, Год журнала: 2025, Номер 52, С. 101009 - 101009

Опубликована: Фев. 27, 2025

Язык: Английский

Процитировано

0
Light-Driven Enzyme Catalysis: Ultrafast Mechanisms and Biochemical Implications DOI Creative Commons

YongLe He,

Marco Barone, Stephen R. Meech

и другие.

Biochemistry, Год журнала: 2025, Номер unknown

Опубликована: Май 29, 2025

Light-activated enzymes are an important class of biocatalysts in which light energy is directly converted into biochemical activity. In most cases the absorbing group isoalloxazine ring embedded flavin cofactor and general two types mechanism operation depending on whether excited chromophore participates catalysis or where photoexcitation triggers conformational changes that modulate activity a downstream output partner. This review will summarize studies DNA photolyase, fatty acid photodecarboxylase (FAP), monooxygenase PqsL, flavin-dependent ene-reductases, radicals generated by excitation used reactions catalyzed these enzymes, blue using FAD (BLUF) oxygen voltage (LOV) domain photoreceptors drives ultrafast structural ultimately result enzyme activation. Recent advances methods such as time-resolved spectroscopy imaging have enabled unprecedented insight dynamics underly light-activated here we highlight how understanding protein not only provides valuable insights natural phototransduction processes but also opens new avenues for engineering consequent applications fields optogenetics.

Язык: Английский

Процитировано

0
Protein-Driven Electron-Transfer Process in a Fatty Acid Photodecarboxylase DOI Creative Commons
Giacomo Londi, Giacomo Salvadori, Patrizia Mazzeo

и другие.

JACS Au, Год журнала: 2024, Номер unknown

Опубликована: Дек. 17, 2024

Naturally occurring photoenzymes are rare in nature, but among them, fatty acid photodecarboxylases derived from Chlorella variabilis (CvFAPs) have emerged as promising photobiocatalysts capable of performing the redox-neutral, light-induced decarboxylation free acids (FAs) into C1-shortened n-alka(e)nes. Using a hybrid QM/MM approach combined with polarizable embedding scheme, we identify structural changes active site and determine energetic landscape forward electron transfer (fET) FA substrate to excited flavin adenine dinucleotide. We obtain charge-transfer diradical structure where water molecule rearranges spontaneously form H-bond interaction flavin, while FA's carboxylate group twists migrates away it. Together, these modifications provide driving force necessary for fET proceed downhill direction. Moreover, by examining R451K mutant is farther core, show that marked reduction electronic coupling counterbalanced an increased force, resulting lifetime similar WT, thereby suggesting resilience process this mutation. Finally, through molecular dynamic simulations, reveal that, following fET, radical occurs within tens picoseconds, overcoming energy barrier ∼0.1 eV. Overall, providing atomistic characterization photoactivation CvFAP, work can be used future protein engineering.

Язык: Английский

Процитировано

1