J. Coleman

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Metabolic interrelationships between carbohydrates lipids and proteins

J. Coleman, 1980 .

Physicochemical and kinetic properties of mushroom tyrosinase.

H. Duckworth, J. Coleman, 1970, The Journal of biological chemistry.

Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster

Joseph E. Coleman, Thomas A. Steitz, David G. Schatz, 1997, Nature Structural Biology.

Structure and mechanism of alkaline phosphatase.

J. Coleman, J E Coleman, 1992, Annual review of biophysics and biomolecular structure.

UME6, a negative regulator of meiosis in saccharomyces cerevisiae, contains a C‐terminal Zn2Cys6 binuclear cluster that binds the URS1 DNA sequence in a zinc‐dependent manner

S. F. Anderson, R. E. Esposito, C. Steber, 1995, Protein science : a publication of the Protein Society.

Current Concepts of the Mechanism of Action of Carbonic Anhydrase

J. Coleman, 1980 .

The catalytic mechanism of carbonic anhydrase.

S. Lindskog, J. Coleman, J E Coleman, 1975, Proceedings of the National Academy of Sciences of the United States of America.

113Cd-1H hetero TOCSY: A method for determining metal—protein connectivities

K. Gardner, J. Coleman, 1994, Journal of biomolecular NMR.

Sequential assignments of the 1H NMR resonances of Zn(II)2 and 113Cd(II)2 derivatives of the DNA-binding domain of the GAL4 transcription factor reveal a novel structural motif for specific DNA recognition.

T. Pan, J. Coleman, 1991, Biochemistry.

Thermal denaturation of T4 gene 32 protein: effects of zinc removal and substitution.

D. Giedroc, K. Williams, J. Sturtevant, 1988, Biochemistry.

The DNA binding domain of GAL4 forms a binuclear metal ion complex.

T. Pan, J. Coleman, 1990, Biochemistry.

1H NMR (500 MHz) of gene 32 protein--oligonucleotide complexes.

K. Williams, J. Casas-Finet, W. Konigsberg, 1984, Biochemistry.

Structure of a promoter for T7 RNA polymerase.

J. Coleman, J. L. Oakley, 1977, Proceedings of the National Academy of Sciences of the United States of America.

Human carbonic anhydrase. Protein conformation and metal ion binding.

J. Coleman, 1965, Biochemistry.

Metal Ion Dependent Binding of Sulphonamide to Carbonic Anhydrase

J. Coleman, 1967, Nature.

Processivity of T7 RNA polymerase requires the C-terminal Phe882-Ala883-COO- or "foot".

P. Peluso, J. Dunn, K. Mookhtiar, 1991, Biochemistry.

Processivity of proteolytically modified forms of T7 RNA polymerase.

C. Martin, J. Coleman, D. Muller, 1988, Biochemistry.

Chapter 8 Phosphomonoesterases

J. Coleman, M. Besman, 1987 .

In vitro selection of small RNAs that bind to Escherichia coli phenylalanyl-tRNA synthetase.

O. Uhlenbeck, T. Pan, J. Coleman, 1994, Journal of molecular biology.

Zinc as a structural and folding element of proteins which interact with DNA

J. Coleman, K. Rodgers, M. Junker, 1997 .

APPENDIX X-RAY STUDIES ON SINGLE CRYSTALS OF ESCHERICHIA COLI ALKALINE PHOSPHATASE

A. W. Hanson, H. Wyckoff, M. Applebury, 1970 .

The Ff gene 5 protein-d(pA)40-60 complex: 1H NMR supports a localized base-binding model.

G. King, J. Coleman, 1988, Biochemistry.

Proton nuclear magnetic resonance (500 MHz) of mono-, di-, tri- and tetradeoxynucleotide complexes of gene 5 protein

J. Coleman, T. O'Connor, 1983 .

Phosphorus-31 and fluorine-19 nuclear magnetic resonance of gene 5 protein-oligonucleotide complexes.

J. Coleman, T. O'Connor, 1982, Biochemistry.

Physiochemical properties of DNA binding proteins: gene 32 protein of T4 and Escherichia coli unwinding protein.

R. Anderson, J. Coleman, 1975, Biochemistry.

Mechanism of action of carbonic anhydrase. Subtrate, sulfonamide, and anion binding.

J. Coleman, 1967, The Journal of biological chemistry.

Metallophosphoryl and Apophosphoryl Alkaline Phosphatases.

J. Coleman, J. Chlebowski, 1976, The Journal of biological chemistry.

Gene 32 protein, the single-stranded DNA binding protein from bacteriophage T4, is a zinc metalloprotein.

D. Giedroc, K. Williams, W. Konigsberg, 1986, Proceedings of the National Academy of Sciences of the United States of America.

Physicochemical properties of cloned nucleocapsid protein from HIV. Interactions with metal ions.

J. Coleman, D. Fitzgerald, 1991, Biochemistry.

Letter: Cadmium-113 Fourier transform nuclear magnetic resonance of cadmium(II) carbonic anhydrases and cadmium(II) alkaline phosphatase.

J. Coleman, I. Armitage, R. T. Pajer, 1976, Journal of the American Chemical Society.

Copper(II) as a probe of the active centers of alkaline phosphatase

S. H. Koenig, I. Bertini, C. Luchinat, 1989 .

Electron spin resonance studies of spin-labeled carbonic anhydrase.

J. Coleman, P. Mushak, 1972, The Journal of biological chemistry.

Zinc metalloproteins involved in replication and transcription.

D. Giedroc, K. Williams, C. Martin, 1986, Journal of inorganic biochemistry.

The catalytic mechanism of carbonic anhydrase.

B. Jonsson, S. Lindskog, J. Coleman, 1973, Proceedings of the National Academy of Sciences of the United States of America.

Chemical reactions of sulfonamides with carbonic anhydrase.

J. Coleman, 1975, Annual review of pharmacology.

Carbon-13 nuclear magnetic resonance as a probe of side chain orientation and mobility in carboxymethylated human carbonic anhydrase B.

J. Prestegard, J. Coleman, I. Armitage, 1978, Biochemistry.

Elasmobranch carbonic anhydrase. Purification and properties of the enzyme from two species of shark.

J. Coleman, J. Maynard, 1971, The Journal of biological chemistry.

Peroxides from autoxidized methyl oleate and linoleate as initiators in the preparation of butadiene-styrene synthetic rubber†

J. Coleman, D. Swern, H. J. Dutton, 1953 .

Reactions of fatty materials with oxygen. XVIII. Catalytic hydrogenation of autoxidized methyl oleate and oleic acid. Preparation of monohydroxystearic acids

J. Coleman, D. Swern, 1955 .

Chemical modifications of functional residues of fd gene 5 DNA-binding protein.

Y. Nakashima, R. Anderson, J. Coleman, 1975, Biochemistry.

1H NMR (500 MHz) identification of aromatic residues of gene 32 protein involved in DNA binding by use of protein containing perdeuterated aromatic residues and by site-directed mutagenesis.

J. W. Chase, Y. Shamoo, K. Williams, 1986, Biochemistry.

T7 RNA polymerase: conformation, functional groups, and promotor binding.

J. Coleman, J. L. Oakley, J. Pascale, 1975, Biochemistry.

Determination of metals in 100 μl sample volumes by atomic absorption analysis using the “spike-height” method of absorbance measurement

H. Duckworth, J. Coleman, 1970 .

Zinc enzymes.

J. Coleman, 1998, Current opinion in chemical biology.

Zinc proteins: enzymes, storage proteins, transcription factors, and replication proteins.

J. Coleman, J E Coleman, 1992, Annual review of biochemistry.

GAL4 transcription factor is not a "zinc finger" but forms a Zn(II)2Cys6 binuclear cluster.

J. Coleman, T. Pan, Tao Pan, 1990, Proceedings of the National Academy of Sciences of the United States of America.

Structural and functional differences between the two intrinsic zinc ions of Escherichia coli RNA polymerase.

D. Giedroc, J. Coleman, 1986, Biochemistry.

EXAFS study of the active site of alkaline phosphatase from E. coli

P. Carloni, S. Mangani, M. Viezzoli, 1992 .

Conformational studies of copper proteins. Pseudomonas blue protein and Polyporus laccase.

J. Coleman, S. P. Tang, Y. Myer, 1968, The Journal of biological chemistry.

113Cd NMR as a probe of the active sites of metalloenzymes

J. Coleman, J. Chlebowski, I. Armitage, 1978 .

Metallocarboxypeptidases: stability constants and enzymatic characteristics.

B. Vallee, J. Coleman, B. Vallée, 1961, The Journal of biological chemistry.

Zn(II)-113Cd(II) and Zn(II)-Mg(II) hybrids of alkaline phosphatase. 31P and 113Cd NMR.

P. Gettins, J. Coleman, 1984, The Journal of biological chemistry.

Escherichia coli co (II) alkaline phsophatase.

M. Applebury, J. Coleman, 1969, The Journal of biological chemistry.

31P NMR of phosphate and phosphonate complexes of metalloalkaline phosphatases.

J. Coleman, J. Chlebowski, I. Armitage, 1976, Journal of Biological Chemistry.

Structure of the active site of carbonic anhydrase as determined by electron spin resonance.

J. Coleman, P. Haffner, 1975, The Journal of biological chemistry.

Cu (II)-carbon bonding in cyanide complexes of copper enzymes. 13C splitting of the Cu(II) electron spin resonance.

J. Coleman, P. Haffner, 1973, The Journal of biological chemistry.

Electron spin resonance of 63 Cu and 65 Cu carbonic anhydrases. Resolution of nitrogen ligand superhyperfine structure.

J. Taylor, J. Coleman, June S. Taylor, 1973, The Journal of biological chemistry.

Nitrogen ligands at the active site of alkaline phosphatase.

J. Taylor, J. Coleman, 1972, Proceedings of the National Academy of Sciences of the United States of America.

The biosynthesis of apo- and metalloalkaline phosphatases of Escherichia coli.

J. Coleman, M. I. Harris, 1968, The Journal of biological chemistry.

Optical rotatory dispersion of copper proteins. Pseudomonas blue protein.

J. Coleman, S. P. Tang, 1967, Biochemical and biophysical research communications.

Phosphate binding to alkaline phosphatase. Metal ion dependence.

M. Applebury, J. Coleman, B. P. Johnson, 1970, The Journal of biological chemistry.

Reactions of Fatty Materials with Oxygen. XII. New Method for Concentrating Long-chain Peroxides2,3

J. Coleman, D. Swern, H. B. Knight, 1952 .

Dissociation Temperatures of Urea Complexes of Long-Chain Fatty Acids, Esters, and Alcohols

J. Coleman, D. Swern, L. P. Witnauer, 1952 .

T7 RNA polymerase does not interact with the 5'-phosphate of the initiating nucleotide.

C. Martin, J. Coleman, 1989, Biochemistry.

Reactions of fatty materials with oxygen. XVII. Some observations on the secondary products of autoxidation of methyl oleate

J. Coleman, D. Swern, H. B. Knight, 1955 .

Reactions of fatty materials with oxygen. XX. Recent developments in the autoxidation of methyl oleate and other monounsaturated fatty materials

J. Coleman, D. Swern, 1955 .

Statistical Comparison of Three Methods for Determining Organic Peroxides

J. Coleman, C. O. Willits, C. Ricciuti, 1955 .

Structure of gene 5 protein-oligodeoxynucleotide complexes as determined by 1H, 19F, and 31P nuclear magnetic resonance.

R. Anderson, R. Ratcliffe, J. Coleman, 1976, Biochemistry.

Tyrosyl-base-phenylalanyl intercalation in gene 5 protein-DNA complexes: proton nuclear magnetic resonance of selectively deuterated gene 5 protein.

J. Coleman, I. Armitage, 1978, Biochemistry.

NMR spectroscopy of 113Cd(II)-substituted gene 32 protein.

D. Giedroc, B. A. Johnson, J. Coleman, 1989, Biochemistry.

31P NMR of alkaline phosphatase. Dependence of phosphate binding stoichiometry on metal ion content.

J. Otvos, J. Coleman, J. Chlebowski, 1979, The Journal of biological chemistry.

Reactions of Fatty Materials with Oxygen. XIV.2 Polarographic and Infrared Spectrophotometric Investigation of Peroxides from Autoxidized Methyl Oleate

J. Coleman, C. O. Willits, D. Swern, 1953 .

Structure of the binuclear metal-binding site in the GAL4 transcription factor.

K. Gardner, T. Pan, J. Coleman, 1991, Biochemistry.

Alkaline phosphatase, solution structure, and mechanism.

P. Gettins, J. Coleman, 2006, Advances in enzymology and related areas of molecular biology.

MULTINUCLEAR NMR APPROACHES TO THE SOLUTION STRUCTURE OF ALKALINE PHOSPHATASE: 13C, 19F, 31P, AND 113Cd NMR*

J. Otvos, J. Coleman, J. Chlebowski, 1979 .

Autoxidation of fatty materials in emulsions. I. Pro-oxidant effect of histidine and trace metals on the oxidation of linoleate esters

J. Coleman, P. A. Wells, J. Hampson, 1962 .

Reactions of fatty materials with oxygen. IX. Analytical study of the autoxidation of methyl oleate

J. Coleman, D. Swern, H. B. Knight, 1951 .

Processivity in early stages of transcription by T7 RNA polymerase.

C. Martin, J. Coleman, Craig T Martin, 1988, Biochemistry.

Dependence of the phosphorylation of alkaline phosphatase by phosphate monoesters on the pKa of the leaving group.

R. Han, J. Coleman, R. Han, 1995, Biochemistry.

31P nuclear magnetic resonance of phosphoenzyme intermediates of alkaline phosphatase.

P. Gettins, J. Coleman, 1983, The Journal of biological chemistry.

Escherichia coli alkaline phosphatase. Metal binding, protein conformation, and quaternary structure.

M. Applebury, J. Coleman, 1969, The Journal of biological chemistry.

Mechanisms of hydrolysis of O-phosphorothioates and inorganic thiophosphate by Escherichia coli alkaline phosphatase.

J. Coleman, J. Chlebowski, 1974, The Journal of biological chemistry.

Allosteric interactions between metal ion and phosphate at the active sites of alkaline phosphatase as determined by 31P NMR and 113Cd NMR.

J. Coleman, J. Chlebowski, I. Armitage, 1977, The Journal of biological chemistry.

Presteady state kinetics of phosphorothioate hydrolysis by alkaline phosphatase. Rate-limiting dephosphorylation at alkaline pH.

J. Coleman, J. Chlebowski, 1972, The Journal of biological chemistry.

Hydrolysis of a stable oxygen ester of phosphorothioic acid by alkaline phosphatase.

J. Coleman, P. Mushak, 1972, Biochemistry.

Isozymes of bovine intestinal alkaline phosphatase.

J. Coleman, M. Besman, Marc BesmanS, 1985, The Journal of biological chemistry.

Physical chemical studies of the structure and function of DNA binding (helix-destabilizing) proteins.

J. Coleman, J. L. Oakley, 1980, CRC critical reviews in biochemistry.

Magnetic circular dichroism of cobalt-copper and zinc-copper bovine superoxide dismutase.

J. Coleman, L. Calabrese, G. Rotillio, 1973, The Journal of biological chemistry.

65Zn(II), 115mCd(II), 60Co(II), and mg(II) binding to alkaline phosphatase of Escherichia coli. Structural and functional effects.

K. Nakamura, J. Coleman, J. Chlebowski, 1983, The Journal of biological chemistry.

113Cd nuclear magnetic resonance of Cd(II) alkaline phosphatases.

P. Gettins, J. Coleman, 1983, The Journal of biological chemistry.

Alkaline phosphatase. 31P NMR probes of the mechanism.

M. Metzler, P. Gettins, J. Coleman, 1985, The Journal of biological chemistry.

Chloride binding to alkaline phosphatase. 113Cd and 35Cl NMR.

P. Gettins, J. Coleman, 1984, The Journal of biological chemistry.

Mn(II) alkaline phosphatase. Electron spin resonance and 31P nuclear magnetic resonance.

J. Coleman, R. Weiner, J. Chlebowski, 1979, The Journal of biological chemistry.

31P NMR of alkaline phosphatase. Saturation transfer and metal-phosphorus coupling.

J. Otvos, J. Alger, J. Coleman, 1979, The Journal of biological chemistry.

T7 RNA polymerase interacts with its promoter from one side of the DNA helix.

C. Martin, J. Coleman, D. Muller, 1989, Biochemistry.

Improved Preparation of 9(10),10(9)-Ketohydroxystearic Acids by Oxidation of Oleic Acid with Potassium Permanganate in Neutral Solution2

J. Coleman, D. Swern, C. Ricciuti, 1956 .

Optical activity associated with the sulfur to metal charge transfer bands of Zn and Cd GAL4

J. Coleman, L. Basile, 1992, Protein science : a publication of the Protein Society.

The function of zinc in gene 32 protein from T4.

D. Giedroc, K. Williams, J. Coleman, 1987, Biochemistry.

Protein chemistry‐nuclear magnetic resonance approach to mapping functional domains in single‐stranded DNA binding proteins

K R Williams, Y. Shamoo, K. Williams, 1986, Journal of cellular biochemistry.

Conformational changes of HIV reverse transcriptase subunits on formation of the heterodimer: correlation with kcat and Km.

J. Coleman, S. Anderson, 1992, Biochemistry.

Carbonic Anhydrase: Zinc and the Mechanism of Catalysis a

J. Coleman, 1984, Annals of the New York Academy of Sciences.

Carbonic anhydrase-azosulfonamide complexes. Spectral properties.

J. Coleman, 1968, The Journal of biological chemistry.

Macaca mulata carbonic anhydrase. Crystallization and physicochemical and enzymatic properties of two isozymes.

J. Coleman, T. Duff, 1966, Biochemistry.

A zinc-binding domain involved in the dimerization of RAG1.

D. Schatz, D. Engelman, D M Engelman, 1996, Journal of molecular biology.

A dimer of the lymphoid protein RAG1 recognizes the recombination signal sequence and the complex stably incorporates the high mobility group protein HMG2.

D. Schatz, L. Ptaszek, I. Villey, 1999, Nucleic acids research.

T7 RNA polymerase: promoter structure and polymerase binding.

A. Sarris, J. Coleman, J. L. Oakley, 1979, Biochemistry.

Kinetic analysis of T7 RNA polymerase-promoter interactions with small synthetic promoters.

C. Martin, J. Coleman, C T Martin, 1987, Biochemistry.

METALLOCARBOXYPEPTIDASE-INHIBITOR COMPLEXES.

B. Vallee, J. Coleman, B. Vallée, 1964, Biochemistry.

Metallocarboxypeptidase-Substrate Complexes*

B. Vallee, J. Coleman, B. Vallée, 1962 .

Apocarboxypeptidase-substrate complexes.

B. Vallee, J. Coleman, B. Vallée, 1962, The Journal of biological chemistry.

Promoter melting by T7 ribonucleic acid polymerase as detected by single-stranded endonuclease digestion.

J. Coleman, J. L. Oakley, R. E. Strothkamp, 1980, Biochemistry.

Zinc fingers, zinc clusters, and zinc twists in DNA-binding protein domains.

B. Vallee, D. Auld, J. Coleman, 1991, Proceedings of the National Academy of Sciences of the United States of America.

The transcription factor LAC9 from Kluyveromyces lactis-like GAL4 from Saccharomyces cerevisiae forms a Zn(II)2Cys6 binuclear cluster.

T. Pan, Y. Halvorsen, R. C. Dickson, 1990, The Journal of biological chemistry.

Cloning, expression, and purification of gene 3 endonuclease from bacteriophage T7.

J. Coleman, T. T. Pham, 1985, Biochemistry.

p10 single-stranded nucleic acid binding protein from murine leukemia virus binds metal ions via the peptide sequence Cys26-X2-Cys29-X4-His34-X4-Cys39.

T. Pan, K. Williams, J. Elliott, 1989, Biochemistry.

Structure and function of the Zn(II) binding site within the DNA-binding domain of the GAL4 transcription factor.

T. Pan, J. Coleman, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Solution structure of the Kluyveromyces lactis LAC9 Cd2Cys6 DNA-binding domain

K. Gardner, J. Coleman, S. Anderson, 1995, Nature Structural Biology.

DNA binding and bending by the transcription factors GAL4(62*) and GAL4(149*)

J. Coleman, K. Rodgers, 1994, Protein science : a publication of the Protein Society.

Role of the zinc(II) ions in the structure of the three-finger DNA binding domain of the Sp1 transcription factor.

J. Coleman, J. Kuwahara, 1990, Biochemistry.

Transcription by T7 RNA polymerase is not zinc-dependent and is abolished on amidomethylation of cysteine-347.

C. Martin, G. King, J. Coleman, 1986, Biochemistry.

The RING Finger Motif of Photomorphogenic Repressor COP1 Specifically Interacts with the RING-H2 Motif of a NovelArabidopsis Protein*

X. Deng, K. Torii, M. Matsui, 1999, The Journal of Biological Chemistry.

Short communication: the N-terminal fragment of Arabidopsis photomorphogenic repressor COP1 maintains partial function and acts in a concentration-dependent manner.

K. Torii, J. Coleman, T. McNellis, 1999, The Plant journal : for cell and molecular biology.

Electron spin resonance of manganese(II)-substituted zinc(II) metalloenzymes.

J. Coleman, F. Goodsaid-Zalduondo, P. Haffner, 1974, The Journal of biological chemistry.

Comparison of cooperative and isolated site binding of T4 gene 32 protein to ssDNA by 1H NMR.

T. Pan, G. King, J. Coleman, 1989, Biochemistry.

Oxidation of olefins with potassium permanganate in oil/water emulsion

J. Coleman, D. Swern, 1958 .

Structure of a promoter for T 7 RNA polymerase *

J. Coleman, J. L. Oakley, 2022 .

Elasmobranch Carbonic Anhydrase

J. Coleman, J. Maynard, 2002 .

T7 ribonucleic acid polymerase-promotor interactions.

J. Coleman, H. Osterman, 1981, Biochemistry.

Catalysis by Metalloenzymes

J. Coleman, 1973 .

Two-dimensional 1H NMR of gene 5 protein indicates that only two aromatic rings interact significantly with oligodeoxynucleotide bases.

G. King, J. Coleman, 1987, Biochemistry.

Magnetic circular dichroism of Co (II) carbonic anhydrase.

J. Coleman, R. V. Coleman, 1972, The Journal of biological chemistry.

Magnetic circular dichroism

J. Coleman, 1976 .

Metalloalkaline phosphatases from Bacillus subtilis: physicochemical and enzymatic properties.

J. Coleman, F. Yoshizumi, 1974, Archives of biochemistry and biophysics.

Protein spherulites.

B. Vallee, J. Coleman, B. Allan, 1960, Science.

Cadmium-113 NMR studies of the DNA binding domain of the mammalian glucocorticoid receptor.

T. Pan, L. Freedman, J. Coleman, 1990, Biochemistry.

Nitrogen and Sulphur at the Active Centre of Carboxypeptidase A

B. Vallee, J. Coleman, ROBERT J. P. Williams, 1961, Nature.

Electron spin resonance of metallocarbonic anhydrases.

J. Taylor, J. Coleman, 1971, The Journal of biological chemistry.

Initiation, elongation, and processivity of carboxyl-terminal mutants of T7 RNA polymerase.

K. Mookhtiar, J. Coleman, L. Gardner, 1997, Biochemistry.

Structure and Mechanism of Copper Oxidases

J. Coleman, 1974 .

Cadmium-113 nuclear magnetic resonance applied to metalloproteins.

J. Coleman, 1993, Methods in enzymology.

1H, 113Cd, and 31P NMR of osteocalcin (bovine gamma-carboxyglutamic acid containing protein).

J. Coleman, R. V. Prigodich, T. O'Connor, 1985, Biochemistry.

Carboxypeptidase A: approaches to the chemical nature of the active center and the mechanisms of action.

J. Riordan, J. Coleman, B. Vallée, 1963, Proceedings of the National Academy of Sciences of the United States of America.

Carbonic anhydrase-azosulfonamide complexes. Optical rotatory dispersion and circular dichroism.

J. Coleman, 1967, Journal of the American Chemical Society.

Autoxidation of fatty materials in emulsion. II. Factors affecting the histidine-catalyzed autoxidation of emulsified methyl linoleate

J. Coleman, J. Hampson, D. Saunders, 1964 .

High spin and low spin forms of Co(II) carbonic anhydrase. Temperature-dependent changes in spin state and coordination geometry.

J. Coleman, P. Haffner, 1973, The Journal of biological chemistry.

113Cd NMR. Arsenate binding to Cd(II) alkaline phosphatase.

P. Gettins, J. Coleman, 1984, Journal of Biological Chemistry.

Magnetic circular dichroism of tryptophanyl residues in proteins. Azurin and carbonic anhydrases.

J. Coleman, T. M. Mcfarland, Joseph E. Coleman, 1972, European journal of biochemistry.

Electron spin resonance studies of carbonic anhydrase: transition metal ions and spin-labeled sulfonamides.

J. Taylor, J. Coleman, P. Mushak, 1970, Proceedings of the National Academy of Sciences of the United States of America.

Organic modifications of metallocarboxypeptidases.

J. Coleman, P. Pulido, B. Vallée, 1966, Biochemistry.