Author

Bengt Reinhammar

Observed names: B Reinhammar, B. REINHAMMAR, B. Reinhammar, Bengt R. M. Reinhammar, Bengt R.M. Reinhammar

Observed institutions: Northwestern University, Leiden University, Uppsala University, Daresbury Laboratory, Chalmers University of Technology, University of Gothenburg, Ruhr University Bochum, University of California, Berkeley

OpenAlex ID: A5010341287

Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes

1990 · P J Kersten, B Kalyanaraman, et al. · Biochemical Journal · 368

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Oxidation-reduction potentials of the electron acceptors in laccases and stellacyanin

1972 · Bengt R.M. Reinhammar · Biochimica et Biophysica Acta (BBA) - Bioenergetics · 301

Large Scale Production and Purification of Laccase from Cultures of the Fungus Polyporus versicolor and some Properties of Laccase A.

1967 · Gösta Fåhraeus, Bengt Reinhammar, et al. · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · 284

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Purification and properties of laccase and stellacyanin from Rhus vernicifera

1970 · Bengt Reinhammar · Biochimica et Biophysica Acta (BBA) - Bioenergetics · 279

The state of copper in stellacyanin and laccase from the lacquer tree Rhus vernicifera

1970 · Bo G. Malmström, Bengt Reinhammar, et al. · Biochimica et Biophysica Acta (BBA) - Bioenergetics · 203

Two forms of copper (II) in fungal laccase

1968 · Bo G. Malmström, Bengt Reinhammar, et al. · Biochimica et Biophysica Acta (BBA) - General Subjects · 135

An X-ray structural study of human ceruloplasmin in relation to ferroxidase activity

1997 · P. F. Lindley, Graeme Card, et al. · JBIC Journal of Biological Inorganic Chemistry · 132

Copper-Containing Oxidases and Superoxide Dismutase

1975 · B.G. Malmstrom, L.-E. Andreasson, et al. · The Enzymes · 126

The Electron‐Accepting Sites in Rhus vernicifera Lacase as Studied by Anaerobic Oxidation‐Reduction Titrations

1971 · Bengt R. M. Reinhammar, Tore I. Vänngåd · European Journal of Biochemistry · 100

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Kinetic studies of Rhus vernicifera laccase

1976 · Lars-Erik Andréasson, Rolf Brändén, et al. · Biochimica et Biophysica Acta (BBA) - Enzymology · 93

The mechanism of electron transfer in laccase-catalysed reactions

1979 · Lars-Erik Andréasson, Bengt Reinhammar · Biochimica et Biophysica Acta (BBA) - Enzymology · 87

Spectroscopic and catalytic properties of rhus vernicifera laccase depleted in type 2 copper

1979 · B Reinhammar · Journal of Inorganic Biochemistry · 82

Cyclic Voltammetry and Electrocatalysis of the Blue Copper Oxidase Polyporus versicolor Laccase.

1998 · Marianne H. Thuesen, Ole Farver, et al. · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · 81

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A new copper(II) electron paramagnetic resonance signal in two laccases and in cytochrome c oxidase.

1980 · B. Reinhammar, R. Malkin, et al. · Journal of Biological Chemistry · 80

Kinetic studies of Rhus vernicifera laccase

1976 · Lars-Erik Andréasson, Bengt Reinhammar · Biochimica et Biophysica Acta (BBA) - Enzymology · 72

Resonance Raman spectra of blue copper proteins: assignments from normal mode calculations and copper-63/copper-65 and H2O/D2O shifts for stellacyanin and laccase

1984 · Lisa Nestor, James A. Larrabee, et al. · Biochemistry · 71

Comparative ENDOR study of six blue copper proteins

1984 · James E. Roberts, John F. Cline, et al. · Journal of the American Chemical Society · 66

Coordination environment for the type 3 copper center of tree laccase and CuB of cytochrome c oxidase as determined by electron nuclear double resonance.

1983 · J Cline, B Reinhammar, et al. · Journal of Biological Chemistry · 66

A 17O-effect on the EPR spectrum of the intermediate in the dioxygen-laccase reaction