2000
DOI: 10.1002/(sici)1097-0290(20000105)67:1<87::aid-bit10>3.0.co;2-8
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The rational design of semisynthetic peroxidases

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Cited by 64 publications
(28 citation statements)
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“…The activity of immobilized phytase was measured using the recently discovered peroxidase activity in the presence of vanadate ( Van de Velde et al, 1998, 2000a. Formate buffer (7 mL, 0.1 M [pH 5.0], containing 10 M Na 3 VO 4 ) and thioanisole (5.0 mM) were added to an appropriate amount of enzyme preparation.…”
Section: Enzyme Activity and Protein Contentmentioning
confidence: 99%
“…The activity of immobilized phytase was measured using the recently discovered peroxidase activity in the presence of vanadate ( Van de Velde et al, 1998, 2000a. Formate buffer (7 mL, 0.1 M [pH 5.0], containing 10 M Na 3 VO 4 ) and thioanisole (5.0 mM) were added to an appropriate amount of enzyme preparation.…”
Section: Enzyme Activity and Protein Contentmentioning
confidence: 99%
“…[4] The underlying principle of artificial metalloenzymes for enantioselective catalysis is based on the incorporation of an active catalyst within a macromolecular host (protein or oligonucleotide) which provides a chiral environment, responsible for the selectivity. [5][6][7][8][9][10] To ensure localization of the catalytic moiety within the macromolecular host, covalent, dative and supramolecular anchoring strategies have successfully been exploited to produce enantioselective hybrid catalysts for ester hydrolysis, [11] dihydroxylation, [12] epoxidation, [13,14] sulfoxidation, [15][16][17][18][19] hydrogenation, [20][21][22][23][24][25][26][27][28] transfer hydrogenation [29,30] and DielsAlder reactions. [31][32][33] Based on Whitesides early report, [20] several groups have been exploiting the biotin-avidin technology to produce artificial hydrogenases for the enantioselective reduction of N-protected dehydroamino acids [21][22][23][24][25][26]28] as well as the reduction via transfer hydrogenation of aromatic ketones.…”
Section: Introductionmentioning
confidence: 99%
“…[1][2][3][4][5] This concept involves placing a metal complex in the chiral microenvironment provided by the biomolecular scaffold using covalent, supramolecular, or dative anchoring strategies. By using a protein scaffold, this method has resulted in a range of enantioselective artificial metalloenzymes that are capable of catalyzing transformations such as transfer hydrogenation, [6] hydrolysis, [7] hydrogenation, [8][9][10] epoxidation, [11,12] sulfoxidation, [13][14][15][16] Diels-Alder reactions, [17,18] transamination, [19] and allylic alkylation. [20] Polynucleotides such as RNA and DNA are arguably some of the most elegant chiral structures in nature and, hence, they are attractive scaffolds for the assembly of enantioselective hybrid catalysts.…”
Section: Introductionmentioning
confidence: 99%