Jing Zhao

Works (7)

Updated: July 5th, 2023 15:44

2017 journal article

Bindings of NO, CO, and O-2 to multifunctional globin type dehaloperoxidase follow the 'sliding scale rule'

Biochemical Journal (London, England : 1984), 474, 3485–3498.

By: G. Wu, J. Zhao, S. Franzen  & A. Tsai

Source: NC State University Libraries
Added: August 6, 2018

2015 article

Distinct Enzyme–Substrate Interactions Revealed by Two Dimensional Kinetic Comparison between Dehaloperoxidase-Hemoglobin and Horseradish Peroxidase

Zhao, J., Lu, C., & Franzen, S. (2015, September 16). The Journal of Physical Chemistry B, Vol. 119, pp. 12828–12837.

By: J. Zhao n, C. Lu* & S. Franzen n 

MeSH headings : Hemoglobins / metabolism; Horseradish Peroxidase / metabolism; Kinetics; Oxidation-Reduction; Peroxidases / metabolism; Substrate Specificity
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Erythrocyte Function and Pathophysiology
TL;DR: DHP is a tortoise, a slow but steady enzyme that wins the evolutionary race against the HRP-type of peroxidase, which is a hare, initially rapid, but flawed for this application because of the protein denaturation under the conditions of the experiment. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2015 article

Measurement of Internal Substrate Binding in Dehaloperoxidase–Hemoglobin by Competition with the Heme–Fluoride Binding Equilibrium

Zhao, J., Moretto, J., Le, P., & Franzen, S. (2015, January 22). The Journal of Physical Chemistry B, Vol. 119, pp. 2827–2838.

By: J. Zhao n, J. Moretto n, P. Le n & S. Franzen n 

MeSH headings : Amino Acids / chemistry; Animals; Anions / chemistry; Binding Sites; Binding, Competitive; Fluorides / chemistry; Halogenation; Heme / chemistry; Hemoglobins / chemistry; Hydrogen Bonding; Hydrogen-Ion Concentration; Indoles / chemistry; Peroxidases / chemistry; Phenols / chemistry; Polychaeta; Protein Binding; Spectrum Analysis
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Neonatal Health and Biochemistry
TL;DR: 2, 4-dibromophenol (2,4-DBP) is identified as the tightest binding substrate discovered thus far, with approximately 20-fold tighter binding affinity than that of 4-bromophenols (4-BP), a known internally binding inhibitor in DHP. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2014 article

Correlation of Heme Binding Affinity and Enzyme Kinetics of Dehaloperoxidase

Le, P., Zhao, J., & Franzen, S. (2014, October 20). Biochemistry, Vol. 53, pp. 6863–6877.

By: P. Le n, J. Zhao n & S. Franzen n 

MeSH headings : Animals; Heme / chemistry; Hemoglobins / chemistry; Kinetics; Peroxidases / chemistry; Polychaeta / enzymology; Protein Binding; Protein Denaturation; Thermodynamics
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Porphyrin Metabolism and Disorders
TL;DR: Thermal denaturation and heme transfer experiments from DHP to HSMb further support the hypothesis that the binding of halophenols to DHP facilitates the removal of the heme, and Kinetic studies verified that DHP B has a catalytic efficiency ∼5-6 times greater than that of DHP A but showed an increased level of substrate inhibition in DHPB for both 2,4,6-TCP and 2, 4, 6-TBP. (via Semantic Scholar)
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6. Clean Water and Sanitation (OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2014 journal article

Peroxygenase and Oxidase Activities of Dehaloperoxidase-Hemoglobin from Amphitrite ornata

Journal of the American Chemical Society, 136(22), 7914–7925.

By: D. Barrios n, J. D’Antonio n, N. McCombs n, J. Zhao n, S. Franzen n , A. Schmidt n, L. Sombers n , R. Ghiladi n 

Contributors: D. Barrios n, . J. D'Antonio n, N. McCombs n, J. Zhao n, S. Franzen n , A. Schmidt n, L. Sombers n , R. Ghiladi n 

MeSH headings : Animals; Catalytic Domain; Hemoglobins / chemistry; Hemoglobins / metabolism; Indoles / chemistry; Indoles / metabolism; Mixed Function Oxygenases / metabolism; Models, Molecular; Oxidoreductases / metabolism; Oxygen / chemistry; Oxygen Consumption; Oxygen Radioisotopes; Polychaeta / enzymology; Protein Conformation
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Metal-Catalyzed Oxygenation Mechanisms
TL;DR: The marine globin dehaloperoxidase‐hemoglobin (DHP) from Amphitrite ornata was found to catalyze the H2O2‐dependent oxidation of monohaloindoles, a previously unreported class of substrate for DHP, and non‐enzymatic and anaerobic controls suggest a novel oxidase activity for D HP. (via Semantic Scholar)
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14. Life Below Water (OpenAlex)
Sources: Web Of Science, NC State University Libraries, ORCID, Crossref
Added: August 6, 2018

2013 article

Kinetic Study of the Inhibition Mechanism of Dehaloperoxidase-Hemoglobin A by 4-Bromophenol

Zhao, J., & Franzen, S. (2013, June 10). The Journal of Physical Chemistry B, Vol. 117, pp. 8301–8309.

By: J. Zhao n & S. Franzen n 

MeSH headings : Crystallography, X-Ray; Enzyme Activation / drug effects; Enzyme Inhibitors / pharmacology; Hemoglobins / chemistry; Kinetics; Mixed Function Oxygenases / antagonists & inhibitors; Mixed Function Oxygenases / chemistry; Models, Molecular; Peroxidases / antagonists & inhibitors; Peroxidases / chemistry; Phenols / pharmacology; Protein Binding / drug effects
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Metal-Catalyzed Oxygenation Mechanisms
TL;DR: Two new species have been identified during the reaction of 4-BP bound form of DHP in the transient-state kinetic experiment by using Singular Value Decomposition (SVD) and global-fitting analysis, and an inhibitor bound intermediate that possesses blue-shifted Soret band and a double peaked Q-band is observed. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2013 article

Structural and Kinetic Study of an Internal Substrate Binding Site in Dehaloperoxidase-Hemoglobin A from Amphitrite ornata

Zhao, J., Serrano, V., Zhao, J., Le, P., & Franzen, S. (2013, March 12). Biochemistry, Vol. 52, pp. 2427–2439.

By: J. Zhao n, V. Serrano n, J. Zhao n, P. Le n & S. Franzen n 

MeSH headings : 2-Propanol / chemistry; Animals; Crystallography, X-Ray; Dimethyl Sulfoxide / chemistry; Hemoglobins / chemistry; Hemoglobins / metabolism; Kinetics; Methanol / chemistry; Models, Molecular; Peroxidases / chemistry; Peroxidases / metabolism; Phenols / chemistry; Polychaeta / chemistry; Polychaeta / enzymology; Polychaeta / metabolism; Protein Conformation
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Erythrocyte Function and Pathophysiology
TL;DR: The X-ray crystal structure is consistent with the presence of an internal active site above the heme α-edge, in which the substrate would be oxidized in two consecutive steps inside the enzyme, followed by attack by H2O via a water channel in the protein. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

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