Construction of biocatalysts using the myoglobin scaffold for the synthesis of indigo from indole

Xu, Jiakun; Okada, Shoji; Fujishiro, Takashi; Ohki, Takahiro; Ueno, Takafumi; Watanabe, Yoshihito

doi:10.1039/c2cy00427e

Cited by 24 publications

(49 citation statements)

References 39 publications

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“…55 Under the conditions examined here, however, neither of these native monofunctional archetypes of the peroxidase and globin families, respectively, were reactive toward 5-Br-indole, a result that highlights the unique reactivity of the dehaloperoxidase-hemoglobin system. Indoleamine 2,3-dioxygenase has also been shown to catalyze the oxidation of indole via a peroxygenase mechanism, however the product distribution is different.…”

Section: Discussionmentioning

confidence: 67%

Peroxygenase and Oxidase Activities of Dehaloperoxidase-Hemoglobin from Amphitrite ornata

et al. 2014

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The marine globin dehaloperoxidase-hemoglobin (DHP) from Amphitrite ornata was found to catalyze the H2O2-dependent oxidation of monohaloindoles, a previously unknown class of substrate for DHP. Using 5-Br-indole as a representative substrate, the major monooxygenated products were found to be 5-Br-2-oxindole and 5-Br-3-oxindolenine. Isotope labeling studies confirmed that the oxygen atom incorporated was derived exclusively from H2O2, indicative of a previously unreported peroxygenase activity for DHP. Peroxygenase activity could be initiated from either the ferric or oxyferrous states with equivalent substrate conversion and product distribution. It was found that 5-Br-3-oxindole, a precursor of the product 5-Br-3-oxindolenine, readily reduced the ferric enzyme to the oxyferrous state, demonstrating an unusual product-driven reduction of the enzyme. As such, DHP returns to the globin-active oxyferrous form after peroxygenase activity ceases. Reactivity with 5-Br-3-oxindole in the absence of H2O2 also yielded 5,5′-Br2-indigo above the expected reaction stoichiometry under aerobic conditions, and O2-concentration studies demonstrated dioxygen consumption. Nonenzymatic and anaerobic controls both confirmed the requirements for DHP and molecular oxygen in the catalytic generation of 5,5′-Br2-indigo, and together suggest a newly identified oxidase activity for DHP.

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Section: Discussionmentioning

confidence: 67%

Peroxygenase and Oxidase Activities of Dehaloperoxidase-Hemoglobin from Amphitrite ornata

et al. 2014

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“…[12] Although great progress has been made in engineering cytochromes to introduce new functions, due to the ease of recombinant overexpression and crystallization, Mb is actually a more favorable scaffold protein for rational heme protein design. Through redesign of the heme-binding active site, Mb has been successfully converted into peroxidases, catalase, peroxygenase (the reader is referred to excellent reviews by Lu et al [1a,b] and Watanabeet al [14] ), manganese peroxidase, heme-copper oxidases (HCOs), and nitric oxidase reductases (NORs). In addition to the introduction of the monooxygenase activity of cyt P450 into Mb, Watanabe and co-workers [14] have recently engineered a His64Asp/ Val68Ile/Ile107Ala Mb variant, which catalyzes the H 2 O 2dependent oxidation of indole, producing indigo, with a k cat value of 72 min À1 .…”

Section: Modification Of the Heme-binding Active Sitementioning

confidence: 99%

“…Through redesign of the heme-binding active site, Mb has been successfully converted into peroxidases, catalase, peroxygenase (the reader is referred to excellent reviews by Lu et al [1a,b] and Watanabeet al [14] ), manganese peroxidase, heme-copper oxidases (HCOs), and nitric oxidase reductases (NORs). In addition to the introduction of the monooxygenase activity of cyt P450 into Mb, Watanabe and co-workers [14] have recently engineered a His64Asp/ Val68Ile/Ile107Ala Mb variant, which catalyzes the H 2 O 2dependent oxidation of indole, producing indigo, with a k cat value of 72 min À1 . In this Mb variant, Asp64 accelerates the reaction with H 2 O 2 and stabilizes the active compound I, while the side chains of Ile68 and Ala107 provide a hydrophobic environment suitable for indole binding.…”

Section: Modification Of the Heme-binding Active Sitementioning

confidence: 99%

Rational Heme Protein Design: All Roads Lead to Rome

Lin

Sawyer

Wang

2013

Chemistry An Asian Journal

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Heme proteins are among the most abundant and important metalloproteins, exerting diverse biological functions including oxygen transport, small molecule sensing, selective CH bond activation, nitrite reduction, and electron transfer. Rational heme protein designs focus on the modification of the heme‐binding active site and the heme group, protein hybridization and domain swapping, and de novo design. These strategies not only provide us with unique advantages for illustrating the structure–property–reactivity–function (SPRF) relationship of heme proteins in nature but also endow us with the ability to create novel biocatalysts and biosensors.

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“…Through redesign of the heme‐binding active site, Mb has been successfully converted into peroxidases, catalase, peroxygenase (the reader is referred to excellent reviews by Lu et al 1a,b. and Watanabeet al 14…”

Section: Introductionmentioning

confidence: 99%

“…), manganese peroxidase, heme‐copper oxidases (HCOs), and nitric oxidase reductases (NORs). In addition to the introduction of the monooxygenase activity of cyt P450 into Mb, Watanabe and co‐workers14 have recently engineered a His64Asp/Val68Ile/Ile107Ala Mb variant, which catalyzes the H 2 O 2 ‐dependent oxidation of indole, producing indigo, with a k cat value of 72 min −1 . In this Mb variant, Asp64 accelerates the reaction with H 2 O 2 and stabilizes the active compound I, while the side chains of Ile68 and Ala107 provide a hydrophobic environment suitable for indole binding.…”

Section: Introductionmentioning

confidence: 99%

Operando Attenuated Total Reflectance FTIR Spectroscopy: Studies on the Different Selectivity Observed in Benzyl Alcohol Oxidation

et al. 2015

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Au, Pd, and AuPd supported on TiO2 were prepared by a sol immobilization route. Operando attenuated total reflectance (ATR) IR spectroscopy and catalytic batch reactor experiments were performed in parallel to elucidate the different catalytic performance of the catalysts in the liquid‐phase oxidation of benzyl alcohol. Pd/TiO2 exhibited a higher activity than AuPd/TiO2 and Au/TiO2, but the modification of Pd with Au demonstrated a significant stability enhancement. ATR‐IR spectroscopy evidenced that the presence of Au facilitates the desorption of byproducts, which thus reduces the extent of deactivation of the active sites caused by the irreversible adsorption of benzoate species. Although benzaldehyde was the main product in both catalysts, the nature of the byproducts differs. Pd/TiO2 favored the deoxygenation of benzyl alcohol to produce toluene as the main byproduct. Conversely, AuPd/TiO2 promoted the transformation of benzaldehyde to benzoic acid.

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Construction of biocatalysts using the myoglobin scaffold for the synthesis of indigo from indole

Cited by 24 publications

References 39 publications

Peroxygenase and Oxidase Activities of Dehaloperoxidase-Hemoglobin from Amphitrite ornata

Peroxygenase and Oxidase Activities of Dehaloperoxidase-Hemoglobin from Amphitrite ornata

Rational Heme Protein Design: All Roads Lead to Rome

Operando Attenuated Total Reflectance FTIR Spectroscopy: Studies on the Different Selectivity Observed in Benzyl Alcohol Oxidation

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