1995 - Member of the National Academy of Sciences
1959 - Fellow of John Simon Guggenheim Memorial Foundation
Lowell P. Hager spends much of his time researching Chloride peroxidase, Organic chemistry, Stereochemistry, Photochemistry and Cytochrome. His Chloride peroxidase research incorporates elements of Haloperoxidase, Catalysis, Enantioselective synthesis and Hydrogen peroxide. His study involves Bromide, Halogenation and Cyanide, a branch of Organic chemistry.
As part of his studies on Stereochemistry, Lowell P. Hager frequently links adjacent subjects like Absorbance. His Photochemistry research incorporates themes from Horseradish peroxidase and Horseradish peroxidase compound I. His work carried out in the field of Cytochrome brings together such families of science as Inorganic chemistry, Ferric, Ligand and Hemeprotein, Heme.
His primary areas of study are Biochemistry, Stereochemistry, Heme, Organic chemistry and Chloride peroxidase. His Stereochemistry research includes themes of Amino acid, Sulfur and Ligation. His Heme study incorporates themes from Cytochrome, Ligand, Photochemistry and Active site.
Lowell P. Hager interconnects Electron paramagnetic resonance and Horseradish peroxidase in the investigation of issues within Photochemistry. His studies in Catalysis, Bromide, Halogenation, Peroxidase and Enzyme are all subfields of Organic chemistry research. The study incorporates disciplines such as Enzyme catalysis and Cytochrome P450 in addition to Chloride peroxidase.
Lowell P. Hager focuses on Catalysis, Organic chemistry, Chloride peroxidase, Stereochemistry and Heme. His studies in Catalysis integrate themes in fields like Combinatorial chemistry, Medicinal chemistry and Hydroxylation. Chloride peroxidase is a subfield of Peroxidase that Lowell P. Hager explores.
His work deals with themes such as Mutant and Halogenation, which intersect with Peroxidase. Lowell P. Hager has included themes like Titanium tetrachloride, Aziridine, Stereocenter and Methyl iodide in his Stereochemistry study. Lowell P. Hager combines subjects such as Photochemistry, Histidine and Active site with his study of Heme.
Catalysis, Chloride peroxidase, Organic chemistry, Stereochemistry and Heme are his primary areas of study. As a member of one scientific family, Lowell P. Hager mostly works in the field of Catalysis, focusing on Hydrogen peroxide and, on occasion, Enzyme, Substrate, Insertion reaction, Indene and Catalase. Chloride peroxidase is the subject of his research, which falls under Peroxidase.
His research in Peroxidase intersects with topics in Reaction mechanism, Mutant, Potassium phosphate and Halogenation. His Heme research incorporates elements of Crystallography, Ligand and Active site. In his study, which falls under the umbrella issue of Active site, Cofactor is strongly linked to Histidine.
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Chloroperoxidase I. ISOLATION AND PROPERTIES OF THE CRYSTALLINE GLYCOPROTEIN
David R. Morris;Lowell P. Hager.
Journal of Biological Chemistry (1966)
Chloroperoxidase. II. Utilization of halogen anions.
Lowell P. Hager;David R. Morris;Frederick S. Brown;Horst Eberwein.
Journal of Biological Chemistry (1966)
Methyl chloride transferase: a carbocation route for biosynthesis of halometabolites
Anne Marie Wuosmaa;Lowell P. Hager.
Science (1990)
Chloroperoxidase compound I: Electron paramagnetic resonance and Mössbauer studies.
Rick Rutter;Lowell P. Hager;Howard Dhonau;Michael Hendrich.
Biochemistry (1984)
Highly enantioselective epoxidation of disubstituted alkenes with hydrogen peroxide catalyzed by chloroperoxidase
Eric J. Allain;Lowell P. Hager;Li Deng;Eric N. Jacobsen.
Journal of the American Chemical Society (1993)
Horseradish peroxidase compound I: evidence for spin coupling between the heme iron and a ‘free’ radical
C.E. Schulz;P.W. Devaney;H. Winkler;P.G. Debrunner.
FEBS Letters (1979)
Chloroperoxidase. VII. Classical peroxidatic, catalatic, and halogenating forms of the enzyme.
John A. Thomas;David R. Morris;Lowell P. Hager.
Journal of Biological Chemistry (1970)
Mössbauer and electron paramagnetic resonance studies of horseradish peroxidase and its catalytic intermediates.
C. E. Schulz;R. Rutter;J. T. Sage;P. G. Debrunner.
Biochemistry (1984)
Chloroperoxidase halogenation reactions. Chemical versus enzymic halogenating intermediates.
R D Libby;J A Thomas;L W Kaiser;L P Hager.
Journal of Biological Chemistry (1982)
A poly(dT)-stimulated ATPase activity associated with simian virus 40 large T antigen.
D Giacherio;L P Hager.
Journal of Biological Chemistry (1979)
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