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Dissimilatory Nitrite and Nitric Oxide Reductases

Chemical reviews, 1996-11, Vol.96 (7), p.2951-2964

Averill, Bruce A

1996

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Crystal Structures of Recombinant Human Purple Acid Phosphatase With and Without an Inhibitory Conformation of the Repression Loop

Journal of molecular biology, 2005-08, Vol.351 (1), p.233-246

2005

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Infantile Hemangiomas Lose Vascular Endothelial Cadherin During Involution: Potential Role in Cell Death?

Plastic and reconstructive surgery. Global open, 2024-05, Vol.12 (5), p.e5832-e5832

2024

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149. Venous Malformation Endothelial Cells Differentially Respond to Laminar Shear Stress

Plastic and reconstructive surgery. Global open, 2023-05, Vol.11 (5S), p.93-93

2023

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20. Therapeutic Targeting of Protein Homeostasis Defects in Venous Malformations

Plastic and reconstructive surgery. Global open, 2023-05, Vol.11 (5S), p.13-14

2023

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Substrate positioning by His92 is important in catalysis by purple acid phosphatase

The FEBS journal, 2005-06, Vol.272 (12), p.2968-2977

2005

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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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Utilization of Healthcare Resources by Vascular Anomaly Patients: An Assessment of Healthcare Burden by Lesion Complexity

Plastic and reconstructive surgery. Global open, 2023-10, Vol.11 (10), p.e5348-e5348

2023

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Electronic Structure of the Perturbed Blue Copper Site in Nitrite Reductase: Spectroscopic Properties, Bonding, and Implications for the Entatic/Rack State

Journal of the American Chemical Society, 1996-08, Vol.118 (33), p.7755-7768

1996

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Nitric Oxide Binding to the Ferri- and Ferroheme States of Nitrophorin 1, a Reversible NO-Binding Heme Protein from the Saliva of the Blood-Sucking Insect, Rhodnius prolixus

Journal of the American Chemical Society, 1999-01, Vol.121 (1), p.128-138

1999

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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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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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Proteins containing oxo-bridged dinuclear iron centers: a bioinorganic perspective

Chemical reviews, 1990-12, Vol.90 (8), p.1447-1467

1990

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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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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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The Fe(III)Zn(II) form of recombinant human purple acid phosphatase is not activated by proteolysis

Journal of inorganic biochemistry, 2005-02, Vol.99 (2), p.521-529

2005

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Direct observation of multiple protonation states in recombinant human purple acid phosphatase

Journal of biological inorganic chemistry, 2005-08, Vol.10 (5), p.550-563

2005

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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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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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Difference Fourier Transform Infrared Evidence for Ester Bonds Linking the Heme Group in Myeloperoxidase, Lactoperoxidase, and Eosinophil Peroxidase

Journal of the American Chemical Society, 1997-11, Vol.119 (47), p.11542-11543

1997

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Electronic and Raman spectroscopic properties of oxo-bridged dinuclear iron centers in proteins and model compounds

Journal of the American Chemical Society, 1989-10, Vol.111 (21), p.8084-8093

1989

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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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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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Dissimilatory Nitrite and Nitric Oxide Reductases

Crystal Structures of Recombinant Human Purple Acid Phosphatase With and Without an Inhibitory Conformation of the Repression Loop

Infantile Hemangiomas Lose Vascular Endothelial Cadherin During Involution: Potential Role in Cell Death?

149. Venous Malformation Endothelial Cells Differentially Respond to Laminar Shear Stress

20. Therapeutic Targeting of Protein Homeostasis Defects in Venous Malformations

Substrate positioning by His92 is important in catalysis by purple acid phosphatase

Denitrification: production and consumption of nitric oxide

Utilization of Healthcare Resources by Vascular Anomaly Patients: An Assessment of Healthcare Burden by Lesion Complexity

Electronic Structure of the Perturbed Blue Copper Site in Nitrite Reductase: Spectroscopic Properties, Bonding, and Implications for the Entatic/Rack State

Nitric Oxide Binding to the Ferri- and Ferroheme States of Nitrophorin 1, a Reversible NO-Binding Heme Protein from the Saliva of the Blood-Sucking Insect, Rhodnius prolixus

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

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

Proteins containing oxo-bridged dinuclear iron centers: a bioinorganic perspective

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

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

The Fe(III)Zn(II) form of recombinant human purple acid phosphatase is not activated by proteolysis

Direct observation of multiple protonation states in recombinant human purple acid phosphatase

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

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

Difference Fourier Transform Infrared Evidence for Ester Bonds Linking the Heme Group in Myeloperoxidase, Lactoperoxidase, and Eosinophil Peroxidase

Electronic and Raman spectroscopic properties of oxo-bridged dinuclear iron centers in proteins and model compounds

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

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

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