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

Creating novel metabolic pathways by protein engineering for bioproduction DOI
Zhou Yu, Yiwei Liu,

Haoran Sun

и другие.

Trends in biotechnology, Год журнала: 2024, Номер unknown

Опубликована: Дек. 1, 2024

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

0