B. Holmquist

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Physical and enzymatic properties of a class III isozyme of human liver alcohol dehydrogenase: chi-ADH.

B. Vallee, F. Wagner, X. Parés, 1984, Biochemistry.

Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes.

H. Jörnvall, B. Vallee, J. Hempel, 1988, Biochemistry.

Fast atom bombardment mass spectrometry and chemical analysis in determinations of acyl‐blocked protein structures

B. Persson, H. Jörnvall, X. Parés, 1990, FEBS letters.

Hydrophobic anion activation of human liver chi chi alcohol dehydrogenase.

B. Vallee, J. Moulis, B. Holmquist, 1991, Biochemistry.

Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation.

H. Jörnvall, K. Engeland, B. Vallee, 1993, Proceedings of the National Academy of Sciences of the United States of America.

A human liver alcohol dehydrogenase enzyme-linked immunosorbent assay method specific for class I, II, and III isozymes.

B. Vallee, B. Holmquist, P. Montavon, 1989, Analytical biochemistry.

Extracellular Fluid Proteins of Goldfish Brain: Evidence for the Presence of Proteases and Esterases

V. Shashoua, B. Holmquist, 1986, Journal of neurochemistry.

cDNA sequence of human class III alcohol dehydrogenase.

H. Jörnvall, E. Fox, B. Vallee, 1989, Biochemical and biophysical research communications.

A continuous spectrophotometric assay for angiotensin converting enzyme.

J. Riordan, B. Holmquist, P. Bünning, 1979, Analytical biochemistry.

Functional residues at the active site of angiotensin converting enzyme.

J. Riordan, B. Holmquist, P. Bünning, 1978, Biochemical and biophysical research communications.

The mechanisms of action of ethanolamine ammonia-lyase, an adenosylcobalamin-dependent enzyme. Evidence that carbon-cobalt bond cleavage is driven in part by conformational alterations of the corrin ring.

B. Babior, J. Krouwer, R. S. Kipnes, 1980, Biochimica et biophysica acta.

Spectral and kinetic studies of metal-substituted Aeromonas aminopeptidase: nonidentical, interacting metal-binding sites.

J. M. Prescott, B. Vallee, F. Wagner, 1985, Biochemistry.

One hundred fold increased activity of Aeromonas aminopeptidase by sequential substitutions with Ni(II) or Cu(II) followed by zinc.

J. M. Prescott, B. Vallee, F. Wagner, 1983, Biochemical and biophysical research communications.

An angiotensin converting enzyme inhibitor is a tight-binding slow substrate of carboxypeptidase A.

J. Riordan, B. Holmquist, M. Martín, 1989, Journal of inorganic biochemistry.

A unique activity assay for carboxypeptidase A in human serum.

J. L. Bethune, B. Holmquist, L. M. Peterson, 1982, Analytical biochemistry.

Circular dichroism and ordered structure of bisnucleoside oligophosphates and their Zn2+ and Mg2+ complexes.

P. Zamecnik, B. Vallee, E. Holler, 1983, Biochemistry.

Oxidation and reduction of 4-hydroxyalkenals catalyzed by isozymes of human alcohol dehydrogenase.

B. Mannervik, B. Vallee, B. Holmquist, 1991, Biochemistry.

Electronic spectroscopy of cobalt angiotensin converting enzyme and its inhibitor complexes.

J. Riordan, R. Bicknell, B. Holmquist, 1987, Biochemistry.

Substrate specificity and kinetic characteristics of angiotensin converting enzyme.

J. Riordan, B. Holmquist, P. Bünning, 1983, Biochemistry.

Characterization of the Active Site of Angiotensin Converting Enzyme

J. Riordan, B. Holmquist, P. Bünning, 1979 .

Thermolysin: a zinc metalloenzyme.

B. Vallee, B. Holmquist, S. Latt, 1969, Biochemical and biophysical research communications.

Rabbit liver class III alcohol dehydrogenase: a cathodic isoform with formaldehyde dehydrogenase activity.

W. Keung, B. Holmquist, L. Kunze, 1995, Alcoholism: Clinical and Experimental Research.

A synthetic peptide encompassing the binding site of the second zinc atom (the 'structural' zinc) of alcohol dehydrogenase.

H. Jörnvall, T. Bergman, B. Vallee, 1992, European journal of biochemistry.

Metal-coordinating substrate analogs as inhibitors of metalloenzymes.

B. Vallee, B. Holmquist, B. Vallée, 1979, Proceedings of the National Academy of Sciences of the United States of America.

Metal substitutions and inhibition of thermolysin: spectra of the cobalt enzyme.

B. Vallee, B. Holmquist, B. Vallée, 1974, The Journal of biological chemistry.

Neocarzinostatin chromophore: purification of the major active form and characterization of its spectral and biological properties.

D. J. Strydom, B. Holmquist, I. Goldberg, 1981, Biochemistry.

Neocarzinostatin: spectral characterization and separation of a non-protein chromophore.

D. J. Strydom, B. Holmquist, I. Goldberg, 1979, Biochemical and biophysical research communications.

Genomic cloning, structure, and regulatory elements of the 1 alpha, 25(OH)2D3 down-regulated gene for cyclic AMP-dependent protein kinase inhibitor.

B. Holmquist, H. Henry, M. Rowland-Goldsmith, 1999, Biochimica et biophysica acta.

Carboxypeptidase of Streptomyces griseus. Implications of its characteristics.

B. Vallee, K. Breddam, B. Holmquist, 1979, Biochemistry.

Energy transfer between terbium (III) and cobalt (II) in thermolysin: a new class of metal--metal distance probes.

B. Vallee, B. Holmquist, W. Horrocks, 1975, Proceedings of the National Academy of Sciences of the United States of America.

Structure of the class II enzyme of human liver alcohol dehydrogenase: combined cDNA and protein sequence determination of the pi subunit.

H. Jörnvall, B. Vallee, K. Larsson, 1987, Biochemistry.

Human liver alcohol dehydrogenase

H. Jörnvall, B. Vallee, J. Hempel, 1984 .

Narcan inhibition of human liver alcohol dehydrogenase.

B. Vallee, B. Holmquist, A. L. Dingley, 1985, Biochemical and biophysical research communications.

Fluorometric assays for isozymes of human alcohol dehydrogenase.

B. Vallee, B. Holmquist, J. Wierzchowski, 1989, Analytical biochemistry.

Physical and enzymatic properties of a class II alcohol dehydrogenase isozyme of human liver: pi-ADH.

B. Vallee, B. Holmquist, M. Morelock, 1984, Biochemistry.

3 beta-Hydroxy-5 beta-steroid dehydrogenase activity of human liver alcohol dehydrogenase is specific to gamma-subunits.

A. J. Mcevily, B. Vallee, D. Auld, 1988, Biochemistry.

Magnetic circular dichroism.

B. Vallee, B. Holmquist, B. Vallée, 1978, Methods in enzymology.

Tryptophan quantitation by magnetic circular dichroism in native and modified proteins.

B. Vallee, B. Holmquist, B. Vallée, 1973, Biochemistry.

Structural and electronic mimics of the active site of cobalt(II)-substituted zinc metalloenzymes.

B. Holmquist, W. Horrocks, J. S. Thompson, 1980, Journal of inorganic biochemistry.

Characterization of the inhibitor complexes of cobalt carboxypeptidase A by electron paramagnetic resonance spectroscopy.

B. Vallee, G. Hanson, J. Pilbrow, 1989, Biochemistry.

5 – The Magnetic Optical Activity of Hemoproteins

B. Holmquist, 1978 .

Cryospectroscopy of intermediates in the mechanism of carboxypeptidase A.

B. Vallee, K. Geoghegan, D. Auld, 1983, Biochemistry.

Magnetic circular dichroism of cobalt metalloenzyme derivatives.

B. Vallee, T. Kaden, B. Holmquist, 1972, Biochemical and biophysical research communications.

Spectral studies of cobalt (II)- and Nickel (II)-metallothionein.

B. Vallee, J. Kägi, B. Holmquist, 1981, Biochemistry.

Asymmetric active site structures in yeast copper,zinc superoxide dismutase. 1. Reconstruction of apo-superoxide dismutase

J. T. Johansen, B. Holmquist, J. Dunbar, 1984 .

Asymmetric active site structures in yeast copper,zinc superoxide dismutase. 2. pH-Dependent incorporation of cobalt into the metal binding sites

J. T. Johansen, B. Holmquist, J. Dunbar, 1984 .

Spectral properties of cobalt carboxypeptidase A. Interaction of the metal atom with anions.

B. Vallee, K. Geoghegan, B. Holmquist, 1983, Biochemistry.

Thioamide substrate probes of metal-substrate interactions in carboxypeptidase A catalysis.

M. D. Bond, B. Vallee, B. Holmquist, 1986, Journal of inorganic biochemistry.

Electrostatic catalysis. II. Comparison of spontaneous and alkaline hydrolytic rate constants for .alpha.-substituted o-nitrophenyl esters

T. C. Bruice, B. Holmquist, 1969 .

The question of the importance of electrostatic catalysis. I. Comparison of the reactivity of o-nitrophenyl hydrogen oxalate and ethyl o-nitrophenyl oxalate toward nucleophiles.

T. C. Bruice, B. Holmquist, 1967, Journal of the American Chemical Society.

The reaction of ribonuclease-A with o-nitrophenyl hydrogen oxalate.

T. C. Bruice, T. Stein, B. Holmquist, 1967, Journal of the American Chemical Society.

Magnetic circular dichroism of non-heme iron proteins.

B. Vallee, B. Holmquist, D. Ulmer, 1973, Biochemical and biophysical research communications.

Magnetic circular dichroism of cobalt(II) complexes

B. Vallee, T. Kaden, B. Holmquist, 2002 .

[2] Elimination of a metals

B. Holmquist, 1988 .

Characterization of the "microprotease" from Bacillus cereus. A zinc neutral endoprotease.

B. Holmquist, 1977, Biochemistry.

Esterase activity of zinc neutral proteases.

B. Vallee, B L Vallee, B. Holmquist, 1976, Biochemistry.

[6] Magnetic circular dichroism

B. Vallee, B. Holmquist, B. Vallée, 1978 .

cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase.

A. Holmgren, K. Larsson, J. Hempel, 1986, Biochemistry.

A spectral study of cobalt(II)-substituted Bacillus cereus phospholipase C.

C. Little, G. Hanson, R. Bicknell, 1986, Biochemistry.

Magnetic circular dichroic spectra of cobalt(II) substituted metalloenzymes.

B. Vallee, T. Kaden, B. Holmquist, 1975, Biochemistry.

Carbonion (ElcB)mechanism of ester hydrolysis. I. Hydrolysis of malonate esters

T. C. Bruice, B. Holmquist, 1969 .

Carbanion mechanism of ester hydrolysis. II. o-Nitrophenyl .alpha.-cyano- and .alpha.-dimethylsulfonioacetate esters

T. C. Bruice, B. Holmquist, 1969 .

Avian alcohol dehydrogenase: the chicken liver enzyme. Primary structure, cDNA-cloning, and relationships to other alcohol dehydrogenases.

H. Jörnvall, E. Fox, B. Vallee, 1990, European journal of biochemistry.

Reversible inactivation and superactivation by covalent modification of thermolysin.

B. Vallee, B. Holmquist, S. Blumberg, 1973, Biochemical and biophysical research communications.

Determination of human serum alcohol dehydrogenase using isozyme-specific fluorescent substrates.

B. Vallee, B. Holmquist, J. Wierzchowski, 1992, Analytical chemistry.

Structural relationships among class I isozymes of human liver alcohol dehydrogenase.

H. Jörnvall, B. Vallee, J. Hempel, 1985, Biochemistry.

Comparison of three classes of human liver alcohol dehydrogenase. Emphasis on different substrate binding pockets.

H. Eklund, H. Jörnvall, E. Horjales, 1990, European Journal of Biochemistry.

chi-ADH is the sole alcohol dehydrogenase isozyme of mammalian brains: implications and inferences.

B. Vallee, B. Holmquist, T. B. Beisswenger, 1985, Proceedings of the National Academy of Sciences of the United States of America.

Human class III alcohol dehydrogenase/glutathione-dependent formaldehyde dehydrogenase

H. Jörnvall, B. Vallee, B. Holmquist, 1991, Journal of protein chemistry.

Basic features of class-I alcohol dehydrogenase: variable and constant segments coordinated by inter-class and intra-class variability. Conclusions from characterization of the alligator enzyme.

B. Persson, H. Jörnvall, T. Bergman, 1993, European journal of biochemistry.

A major form of reptilian-line alcohol dehydrogenase exhibits class I properties and reveals evolutionary relationships of the enzyme family

B. Persson, H. Jörnvall, T. Bergman, 1992 .

Characteristics of mammalian class III alcohol dehydrogenases, an enzyme less variable than the traditional liver enzyme of class I.

H. Jörnvall, B. Vallee, B. Holmquist, 1989, Biochemistry.

A synthetic approach to analysis of the structural zinc site of alcohol dehydrogenase.

H. Jörnvall, T. Bergman, T. Härd, 1993, Advances in experimental medicine and biology.

Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase.

B. Vallee, B. Holmquist, W. Gutheil, 1992, Biochemistry.

Carboxypeptidase A. Differences in the mechanisms of ester and peptide hydrolysis.

D. Auld, B. Holmquist, 1974, Biochemistry.

Effects of mechanism-based reversible inhibitors on the metal environment of cobalt(II)carboxypeptidase A: an electronic spectral study.

J. Riordan, B. Holmquist, M. Martín, 1989, Journal of inorganic biochemistry.

Esterase activity of rabbit pulmonary angiotensin converting enzyme.

J. Riordan, B. Holmquist, W. Keung, 1980, Biochemical and biophysical research communications.

Electrostatic catalysis. III. Comparison of the reactivity of .alpha.-substituted o-nitrophenyl esters with anionic and amine nucleophiles

T. C. Bruice, B. Holmquist, 1969 .

Superactivation of neutral proteases: acylation with N-hydroxysuccinimide esters.

B. Vallee, B. Holmquist, S. Blumberg, 1976, Biochemistry.

Magnetic circular dichroism of biological molecules.

J. Sutherland, B. Holmquist, 1980, Annual review of biophysics and bioengineering.

HUMAN LIVER ALCOHOL DEHYDROGENASE: THE PRIMARY STRUCTURE OF THE β1β1 ISOENZYME

H. Jörnvall, B. Vallee, J. Hempel, 1984 .

Anion activation of angiotensin converting enzyme: dependence on nature of substrate.

J F Riordan, R Shapiro, R. Shapiro, 1983, Biochemistry.

Iron-sulfur centers in lactyl-CoA dehydratase

G. Hanson, R. Kuchta, B. Holmquist, 1986 .

Enzyme-Linked Immunosorbent Assay for the Detection of Mercury in Environmental Matrices

D. Wylie, B. Holmquist, L. Carlson, 1996 .

Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase.

K. Engeland, B. Vallee, J. Moulis, 1993, Biochemistry.

Human liver class III alcohol and glutathione dependent formaldehyde dehydrogenase are the same enzyme.

B. Vallee, B. Holmquist, B. Vallée, 1991, Biochemical and biophysical research communications.

Acetylated N‐terminal structures of class III alcohol dehydrogenases Differences among the three enzyme classes

H. Jörnvall, B. Vallee, X. Parés, 1987, FEBS letters.

Hydrolysis of peptides by carboxypeptidase A: equilibrium trapping of the ES2 intermediate.

K. Geoghegan, G. Hanson, D. Auld, 1986, Biochemistry.

Modulation of Thermolysin Activity. Reversibility of Inactivation and Superactivation

B. Holmquist, S. Blumberg, B. Vallée, 1974 .

Cryospectrokinetic characterization of intermediates in biochemical reactions: carboxypeptidase A.

K. Geoghegan, D. Auld, A. Galdes, 1984, Proceedings of the National Academy of Sciences of the United States of America.

Fe-S centers in lactyl-CoA dehydratase.

G. Hanson, R. Kuchta, B. Holmquist, 1986, Biochemistry.