Shu Jiang

Works (2)

Updated: July 5th, 2023 15:44

2013 article

The role of T56 in controlling the flexibility of the distal histidine in dehaloperoxidase-hemoglobin from Amphitrite ornata

Jiang, S., Wright, I., Swartz, P., & Franzen, S. (2013, June 20). Biochimica Et Biophysica Acta (BBA) - Proteins and Proteomics, Vol. 1834, pp. 2020–2029.

By: S. Jiang n, I. Wright  n, P. Swartz n & S. Franzen n 

author keywords: Enzyme kinetics; Catalytic efficiency; Hemichrome; Resonance Raman; Molecular dynamics
MeSH headings : Animals; Biocatalysis; Heme / chemistry; Hemoglobins / chemistry; Hemoglobins / genetics; Histidine / chemistry; Histidine / genetics; Iron / chemistry; Kinetics; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Peroxidases / chemistry; Peroxidases / genetics; Polychaeta / chemistry; Polychaeta / enzymology; Recombinant Proteins / chemistry; Recombinant Proteins / genetics; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; Thermodynamics; Threonine / chemistry; Threonine / genetics
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Erythrocyte Function and Pathophysiology
TL;DR: It is confirmed that subtle changes in the conformation of H55 affect the catalytic efficiency of DHP, and a balance of enzymatic rate and protein stability with respect to hemichrome formation appears to be optimum in wild type DHP (WT-DHP). (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2012 article

Catalytic efficiency of dehaloperoxidase A is controlled by electrostatics – application of the vibrational Stark effect to understand enzyme kinetics

Schkolnik, G., Utesch, T., Zhao, J., Jiang, S., Thompson, M. K., Mroginski, M.-A., … Franzen, S. (2012, December 19). Biochemical and Biophysical Research Communications, Vol. 430, pp. 1011–1015.

By: G. Schkolnik *, T. Utesch *, J. Zhao n, S. Jiang n, M. Thompson n, M. Mroginski *, P. Hildebrandt *, S. Franzen n 

author keywords: Vibrational Stark effect; Hemoglobin; 4-mercaptobenzonitrile; Enzyme kinetics; Electric field
MeSH headings : Animals; Catalysis; Kinetics; Mutation; Peroxidase / chemistry; Peroxidase / genetics; Peroxidases / chemistry; Peroxidases / genetics; Polychaeta / enzymology; Protein Conformation; Spectroscopy, Fourier Transform Infrared; Static Electricity; Vibration
topics (OpenAlex): Hemoglobin structure and function; Spectroscopy and Quantum Chemical Studies; Electron Spin Resonance Studies
TL;DR: By labeling the protein with 4-mercaptobenzonitrile (MBN), a Stark probe molecule, this work provides further evidence that the diffusion control of the catalytic process arises from the electrostatic repulsion between the enzyme and the negatively charged substrate. (via Semantic Scholar)
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UN Sustainable Development Goal Categories
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

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