4 publications

4 publications

Autoxidation of Ascorbic Acid Catalyzed by a Semisynthetic Enzyme

Kaiser, E.T.

Biopolymers 1990, 29, 39-43, 10.1002/bip.360290107

The semisyntehtic enzyme 6 was prepared by alkylation of the cysteine‐25 sulfhydryl group of papain with the bipyridine 5 and was shown to stoichiometrically bind copper ion; 7 catalyzed the autoxidation of ascorbic acid derivatives with saturation kinetics approximately 20‐fold faster than a model system using 3‐Cu(II).


Metal: Cu
Ligand type: Bipyridine
Host protein: Papain (PAP)
Anchoring strategy: Covalent
Optimization: ---
Reaction: Oxidation
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Flavohemoglobin: A Semisynthetic Hydroxylase Acting in the Absence of Reductase

Kaiser, E.T.

J. Am. Chem. Soc. 1987, 109, 606-607, 10.1021/ja00236a062

n/a


Metal: Fe
Ligand type: Porphyrin
Host protein: Hemoglobin
Anchoring strategy: ---
Optimization: ---
Max TON: ---
ee: ---
PDB: ---
Notes: ---

Helichrome: Synthesis and Enzymatic Activity of a Designed Hemeprotein

Kaiser, E.T.; Sasaki, T.

J. Am. Chem. Soc. 1989, 111, 380-381, 10.1021/ja00183a065

n/a


Metal: Fe
Ligand type: Porphyrin
Host protein: Artificial construct
Anchoring strategy: Covalent
Optimization: ---
Max TON: ---
ee: ---
PDB: ---
Notes: Only 60 amino acids

Studies on the Oxidase Activity of Copper (II) Carboxypeptidase A

Kaiser, E.T.

J. Chem. Soc., Chem. Commun. 1976, 830, 10.1039/C39760000830

Copper(II) carboxypeptidase A catalyses the oxidation of ascorbic acid and this reaction is inhibited by α-benzylsuccinate, a known inhibitor of the thiolesterase action of the copper enzyme; the pH dependencies of kcat and kcat/Km are similar near pH 7 to those seen for the peptidase and esterase activities of native carboxypeptidase A.


Metal: Cu
Ligand type: Amino acid
Host protein: Carboxypeptidase A
Anchoring strategy: Metal substitution
Optimization: ---
Reaction: Oxidation
Max TON: ---
ee: ---
PDB: ---
Notes: Oxidation of vitamin C