Physicochemical and biochemical properties of synthetic zinc 131-(un)substituted chlorophyll-a derivatives

Hirose, Mitsuaki; Harada, Jiro; Maeda, Hiroaki; Tamiaki, Hitoshi

doi:10.1016/j.tet.2021.132151

Cited by 3 publications

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“…If the latter release-and-capture reaction occurred, some C13 2 -COOH intermediates should have been detected in previous reports, in which in vitro BciC-catalyzed reactions were performed with various Chl derivatives (Figure S18). ,,, However, no C13 2 -COOH intermediate bearing the natural E ring had been detected, except in the BciC enzymatic reactions of Chl analogues possessing the 13 1 -hydroxy, 13 2 -methylene, or 13 2 -ethylene group (Figure S1). , Hence, the former mechanism is preferable where the C13 2 -COOH product was decarboxylated through the conformational rotation inside the active site of the BciC enzyme.…”

Section: Discussionmentioning

confidence: 99%

Predicted Structure of the BciC Enzyme Catalyzing the Removal of the C13²-Methoxycarbonyl Group for Biosynthesis of Chlorosomal Chlorophylls: A Mechanism for Dual Catalytic Functions of Hydrolysis and Decarboxylation inside Its Active Site

et al. 2023

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Green photosynthetic bacteria, one of the phototrophs, have the largest and most efficient light-harvesting antenna systems, called chlorosomes. The core part of chlorosomes consists of unique bacteriochlorophyll c/d/e molecules. In the biosynthetic pathway of these molecules, a BciC enzyme catalyzes the removal of the C13 2 -methoxycarbonyl group of chlorophyllide a. Two sequential reactions have been proposed for the BciC enzymatic demethoxycarbonylation: the BciC enzyme would catalyze the hydrolysis of the C13 2 -methoxycarbonyl group, and the resulting carboxylic acid would be rapidly decarboxylated to generate pyrochlorophyllide a. In this study, we computationally predicted the three-dimensional structure of the BciC protein. Its active site was proposed based on structural analysis using docking simulation. In vitro enzymatic reaction assays of mutated BciC supported the prediction. The BciC enzymatic hydrolysis would be an aspartic/glutamic acid hydrolase, which involves the amino residues E85 and D180. Furthermore, Y58 and H126 might depend on stabilization and/or recognition with the substrate. Most importantly, H137 would protonate 13-C�O or deprotonate C13 2 -COOH in the hydrolyzed product to promote decarboxylation. In conclusion, the BciC enzyme has the dual functions of hydrolysis and decarboxylation.

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Section: Discussionmentioning

confidence: 99%

Predicted Structure of the BciC Enzyme Catalyzing the Removal of the C13²-Methoxycarbonyl Group for Biosynthesis of Chlorosomal Chlorophylls: A Mechanism for Dual Catalytic Functions of Hydrolysis and Decarboxylation inside Its Active Site

et al. 2023

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Synthesis of C3-substituted chlorophyll-a derivatives fused by a π-conjugated E-ring and their physical properties with unique near-infrared absorption

Hashimoto,

Yamashita,

Hara

et al. 2024

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Difluoroboron complexes of peripheral β-diketonates in cyclopheophorbides: Their syntheses and optical properties

et al. 2022

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Physicochemical and biochemical properties of synthetic zinc 131-(un)substituted chlorophyll-a derivatives

Cited by 3 publications

References 44 publications

Predicted Structure of the BciC Enzyme Catalyzing the Removal of the C13²-Methoxycarbonyl Group for Biosynthesis of Chlorosomal Chlorophylls: A Mechanism for Dual Catalytic Functions of Hydrolysis and Decarboxylation inside Its Active Site

Predicted Structure of the BciC Enzyme Catalyzing the Removal of the C13²-Methoxycarbonyl Group for Biosynthesis of Chlorosomal Chlorophylls: A Mechanism for Dual Catalytic Functions of Hydrolysis and Decarboxylation inside Its Active Site

Synthesis of C3-substituted chlorophyll-a derivatives fused by a π-conjugated E-ring and their physical properties with unique near-infrared absorption

Difluoroboron complexes of peripheral β-diketonates in cyclopheophorbides: Their syntheses and optical properties

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Physicochemical and biochemical properties of synthetic zinc 131-(un)substituted chlorophyll-a derivatives

Cited by 3 publications

References 44 publications

Predicted Structure of the BciC Enzyme Catalyzing the Removal of the C132-Methoxycarbonyl Group for Biosynthesis of Chlorosomal Chlorophylls: A Mechanism for Dual Catalytic Functions of Hydrolysis and Decarboxylation inside Its Active Site

Predicted Structure of the BciC Enzyme Catalyzing the Removal of the C132-Methoxycarbonyl Group for Biosynthesis of Chlorosomal Chlorophylls: A Mechanism for Dual Catalytic Functions of Hydrolysis and Decarboxylation inside Its Active Site

Synthesis of C3-substituted chlorophyll-a derivatives fused by a π-conjugated E-ring and their physical properties with unique near-infrared absorption

Difluoroboron complexes of peripheral β-diketonates in cyclopheophorbides: Their syntheses and optical properties

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Predicted Structure of the BciC Enzyme Catalyzing the Removal of the C13²-Methoxycarbonyl Group for Biosynthesis of Chlorosomal Chlorophylls: A Mechanism for Dual Catalytic Functions of Hydrolysis and Decarboxylation inside Its Active Site

Predicted Structure of the BciC Enzyme Catalyzing the Removal of the C13²-Methoxycarbonyl Group for Biosynthesis of Chlorosomal Chlorophylls: A Mechanism for Dual Catalytic Functions of Hydrolysis and Decarboxylation inside Its Active Site