Mechanistic Study on the Oxidation of Anthocyanidin Synthase by Quantum Mechanical Calculation

Nakajima, Jun–ichiro; Sato, Yoshiharu; Hoshino, Tyuji; Yamazaki, Mami; Saito, Kazuki

doi:10.1074/jbc.m600303200

Cited by 31 publications

(31 citation statements)

References 45 publications

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“…Interestingly, we found that the catalytic reduction peak potential of H 2 O 2 was almost same with that of O 2. This phenomenon was also observed in other researches [24,25,27,28] [29,30]. As interpreted in [25], the as-produced O 2 makes the similarity of electrochemical catalytic behavior between O 2 and H 2 O 2 .…”

Section: Resultssupporting

confidence: 69%

Direct Electrochemistry of Horseradish Peroxidase Immobilized in Calcium Carbonate Microsphere Doped with Phospholipids

Liu

et al. 2008

Electroanalysis

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Protein electrochemistry affords a direct method to study the biological electron transfer processes. However, supplying a biocompatible environment to maintain the native state of protein is all-important and challengeable. Here, we chose vaterite, one of the crystalline polymorphs of calcium carbonate, with highly porous nature and large specific surface area, which was doped with phospholipids, as the matrix to immobilize horseradish peroxidase (HRP). The integrity of HRP was kept during the simple immobilization procedure. By virtue of this organic/inorganic complex matrix, the direct electrochemistry of HRP was realized, and the activity of HRP for catalyzing reduction of O 2 and H 2 O 2 was preserved.

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Section: Resultssupporting

confidence: 69%

Direct Electrochemistry of Horseradish Peroxidase Immobilized in Calcium Carbonate Microsphere Doped with Phospholipids

Liu

et al. 2008

Electroanalysis

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“…These additions occur at the ␦-meso position of the heme, whereas reactions of alkylhydrazines with myoglobin produce ␥-meso-alkylated hemes (44). Particularly relevant is the observation that the autoinactivation of horseradish peroxidase in the presence of excess oxidizing agent involves hydroxylation at a meso position, a reaction in which a transient (presumably isoporphyrin) species with an absorption at 940 nm has been detected (45,46).…”

Section: Discussionmentioning

confidence: 99%

Isoporphyrin Intermediate in Heme Oxygenase Catalysis

Evans

Niemevz

Buldain

et al. 2008

Journal of Biological Chemistry

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Human heme oxygenase-1 (hHO-1) catalyzes the O 2 -and NADPH-dependent oxidation of heme to biliverdin, CO, and free iron. The first step involves regiospecific insertion of an oxygen atom at the ␣-meso carbon by a ferric hydroperoxide and is predicted to proceed via an isoporphyrin -cation intermediate. Here we report spectroscopic detection of a transient intermediate during oxidation by hHO-1 of ␣-meso-phenylheme-IX, ␣-meso-(p-methylphenyl)-mesoheme-III, and ␣-meso-(p-tri-

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“…ANS, a member of the 2-oxoglutarate-dependent dioxygenases, catalyzes the conversion of colorless leucoanthocyanidins to the colored anthocyanidins (Nakajima et al, 2006). Connecting unstable substrates (leucoanthocyanidins) with unstable products (anthocyanidins) makes the biochemical investigation of ANS enzymes a very challenging task (Nakajima et al, 2001;Saito et al, 1999).…”

Section: Comparison Of Ans Activity From Different Plant Speciesmentioning

confidence: 99%

High‐yield anthocyanin biosynthesis in engineered Escherichia coli

Yan¹,

Li²,

Koffas³

2007

Biotech & Bioengineering

117

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Anthocyanins are red, purple, or blue plant water-soluble pigments. In the past two decades, anthocyanins have received extensive studies for their anti-oxidative, anti-inflammatory, anti-cancer, anti-obesity, anti-diabetic, and cardioprotective properties. In the present study, anthocyanin biosynthetic enzymes from different plant species were characterized and employed for pathway construction leading from inexpensive precursors such as flavanones and flavan-3-ols to anthocyanins in Escherichia coli. The recombinant E. coli cells successfully achieved milligram level production of two anthocyanins, pelargonidin 3-O-glucoside (0.98 mg/L) and cyanidin 3-O-gluside (2.07 mg/L) from their respective flavanone precursors naringenin and eriodictyol. Cyanidin 3-O-glucoside was produced at even higher yields (16.1 mg/L) from its flavan-3-ol, (+)-catechin precursor. Further studies demonstrated that availability of the glucosyl donor, UDP-glucose, was the key metabolic limitation, while product instability at normal pH was also identified as a barrier for production improvement. Therefore, various optimization strategies were employed for enhancing the homogenous synthesis of UDP-glucose in the host cells while at the same time stabilizing the final anthocyanin product. Such optimizations included culture medium pH adjustment, the creation of fusion proteins and the rational manipulation of E. coli metabolic network for improving the intracellular UDP-glucose metabolic pool. As a result, production of pelargonidin 3-O-glucoside at 78.9 mg/L and cyanidin 3-O-glucoside at 70.7 mg/L was achieved from their precursor flavan-3-ols without supplementation with extracellular UDP-glucose. These results demonstrate the efficient production of the core anthocyanins for the first time and open the possibility for their commercialization for pharmaceutical and nutraceutical applications.

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Mechanistic Study on the Oxidation of Anthocyanidin Synthase by Quantum Mechanical Calculation

Cited by 31 publications

References 45 publications

Direct Electrochemistry of Horseradish Peroxidase Immobilized in Calcium Carbonate Microsphere Doped with Phospholipids

Direct Electrochemistry of Horseradish Peroxidase Immobilized in Calcium Carbonate Microsphere Doped with Phospholipids

Isoporphyrin Intermediate in Heme Oxygenase Catalysis

High‐yield anthocyanin biosynthesis in engineered Escherichia coli

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