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Denitrification: production and consumption of nitric oxide

Applied and environmental microbiology, 1994-04, Vol.60 (4), p.1053-1058

1994

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Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions

Trends in biochemical sciences (Amsterdam. Regular ed.), 1992-03, Vol.17 (3), p.105-110

1992

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Mutational Analysis of the Interaction between Active Site Residues and the Loop Region in Mammalian Purple Acid Phosphatases

Biochemistry (Easton), 2001-09, Vol.40 (38), p.11614-11622

2001

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Immunological identification and distribution of dissimilatory heme cd1 and nonheme copper nitrite reductases in denitrifying bacteria

Applied and Environmental Microbiology, 1989-11, Vol.55 (11), p.2924-2931

1989

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Evidence that the Type 2 copper centers are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase

Biochemical and biophysical research communications, 1992-09, Vol.187 (3), p.1529-1535

1992

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Characterization of the structural gene encoding a copper-containing nitrite reductase and homology of this gene to DNA of other denitrifiers

Applied and Environmental Microbiology, 1993-01, Vol.59 (1), p.250-254

1993

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Evidence for an NO‐rebound, mechanism for production of N2O from nitrite by the copper‐containing nitrite reductase from Achromobacter cycloclastes

FEBS letters, 1991-10, Vol.291 (1), p.41-44

1991

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An enzyme with a double identity: purple acid phosphatase and tartrate‐resistant acid phosphatase

The FASEB journal, 1990-09, Vol.4 (12), p.3009-3014

1990

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Mutants of Pseudomonas fluorescens deficient in dissimilatory nitrite reduction are also altered in nitric oxide reduction

Journal of Bacteriology, 1992-04, Vol.174 (8), p.2560-2564

1992

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Electron paramagnetic resonance studies on the high-salt form of bovine spleen purple acid phosphatase

Biochemistry (Easton), 1992-10, Vol.31 (40), p.9603-9608

1992

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Characterization of Tn5 mutants deficient in dissimilatory nitrite reduction in Pseudomonas sp. strain G-179, which contains a copper nitrite reductase

Journal of Bacteriology, 1992-10, Vol.174 (20), p.6653-6658

1992

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Isolation of a high specific activity pink, monomeric nitrous oxide reductase from Achromobacter cycloclastes

Biochemical and biophysical research communications, 1990-01, Vol.166 (2), p.729-735

1990

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Spectroscopic and kinetics studies of a high-salt-stabilized form of the purple acid phosphatase from bovine spleen

Biochemistry (Easton), 1991-03, Vol.30 (12), p.3025-3034

1991

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Internal friction of amine-intercalated TaS2

Journal of materials science, 1998-04, Vol.33 (7), p.1949-1954

1998

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Evidence for a copper-nitrosyl intermediate in denitrification by the copper-containing nitrite reductase of Achromobacter cycloclastes

Journal of the American Chemical Society, 1989-03, Vol.111 (6), p.2322-2323

1989

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Purification and properties of the native form of the purple acid phosphatase from bovine spleen

Biochemistry (Easton), 1993-08, Vol.32 (32), p.8120-8129

1993

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Fluoride Inhibition of Bovine Spleen Purple Acid Phosphatase: Characterization of a Ternary Enzyme−Phosphate−Fluoride Complex as a Model for the Active Enzyme−Substrate−Hydroxide Complex

Biochemistry (Easton), 1999-08, Vol.38 (31), p.9926-9936

1999

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Ga3+ as a Functional Substitute for Fe3+: Preparation and Characterization of the Ga3+Fe2+ and Ga3+Zn2+ Forms of Bovine Spleen Purple Acid Phosphatase

Biochemistry (Easton), 1998-06, Vol.37 (23), p.8490-8497

1998

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X-ray absorption studies of the purple acid phosphatase from beef spleen

Inorganic chemistry, 1986-07, Vol.25 (16), p.2781-2785

1986

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Evidence for Nonbridged Coordination of p-Nitrophenyl Phosphate to the Dinuclear Fe(III)−M(II) Center in Bovine Spleen Purple Acid Phosphatase during Enzymatic Turnover

Biochemistry (Easton), 1999-08, Vol.38 (31), p.9914-9925

1999

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The Activity of Oxidized Bovine Spleen Purple Acid Phosphatase Is Due to an Fe(III)Zn(II) ‘Impurity

Biochemistry (Easton), 1998-08, Vol.37 (32), p.11223-11231

1998

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Isotope labeling studies on the mechanism of N-N bond formation in denitrification

The Journal of biological chemistry, 1986-07, Vol.261 (21), p.9652-9656

1986

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The Highly Exposed Loop Region in Mammalian Purple Acid Phosphatase Controls the Catalytic Activity

Chembiochem : a European journal of chemical biology, 2001-05, Vol.2 (5), p.355-363

2001

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A spectrophotometric assay for dissimilatory nitrite reductases

Analytical biochemistry, 1988-08, Vol.172 (2), p.420-426

1988

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Multiple binding sites for tetrahedral oxyanion inhibitors of bovine spleen purple acid phosphatase

Biochemistry (Easton), 1992-03, Vol.31 (12), p.3033-3037

1992

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Denitrification: production and consumption of nitric oxide

Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions

Mutational Analysis of the Interaction between Active Site Residues and the Loop Region in Mammalian Purple Acid Phosphatases

Immunological identification and distribution of dissimilatory heme cd1 and nonheme copper nitrite reductases in denitrifying bacteria

Evidence that the Type 2 copper centers are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase

Characterization of the structural gene encoding a copper-containing nitrite reductase and homology of this gene to DNA of other denitrifiers

Evidence for an NO‐rebound, mechanism for production of N2O from nitrite by the copper‐containing nitrite reductase from Achromobacter cycloclastes

An enzyme with a double identity: purple acid phosphatase and tartrate‐resistant acid phosphatase

Mutants of Pseudomonas fluorescens deficient in dissimilatory nitrite reduction are also altered in nitric oxide reduction

Electron paramagnetic resonance studies on the high-salt form of bovine spleen purple acid phosphatase

Characterization of Tn5 mutants deficient in dissimilatory nitrite reduction in Pseudomonas sp. strain G-179, which contains a copper nitrite reductase

Isolation of a high specific activity pink, monomeric nitrous oxide reductase from Achromobacter cycloclastes

Spectroscopic and kinetics studies of a high-salt-stabilized form of the purple acid phosphatase from bovine spleen

Internal friction of amine-intercalated TaS2

Evidence for a copper-nitrosyl intermediate in denitrification by the copper-containing nitrite reductase of Achromobacter cycloclastes

Purification and properties of the native form of the purple acid phosphatase from bovine spleen

Fluoride Inhibition of Bovine Spleen Purple Acid Phosphatase: Characterization of a Ternary Enzyme−Phosphate−Fluoride Complex as a Model for the Active Enzyme−Substrate−Hydroxide Complex

Ga3+ as a Functional Substitute for Fe3+: Preparation and Characterization of the Ga3+Fe2+ and Ga3+Zn2+ Forms of Bovine Spleen Purple Acid Phosphatase

X-ray absorption studies of the purple acid phosphatase from beef spleen

Evidence for Nonbridged Coordination of p-Nitrophenyl Phosphate to the Dinuclear Fe(III)−M(II) Center in Bovine Spleen Purple Acid Phosphatase during Enzymatic Turnover

The Activity of Oxidized Bovine Spleen Purple Acid Phosphatase Is Due to an Fe(III)Zn(II) ‘Impurity

Isotope labeling studies on the mechanism of N-N bond formation in denitrification

The Highly Exposed Loop Region in Mammalian Purple Acid Phosphatase Controls the Catalytic Activity

A spectrophotometric assay for dissimilatory nitrite reductases

Multiple binding sites for tetrahedral oxyanion inhibitors of bovine spleen purple acid phosphatase

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