2013 journal article

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

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 430(3), 1011–1015.

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

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
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)
UN Sustainable Development Goal Categories
Sources: Web Of Science, ORCID
Added: August 6, 2018

2013 journal article

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

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1834(10), 2020–2029.

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

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
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)
UN Sustainable Development Goal Categories
Sources: Web Of Science, ORCID
Added: August 6, 2018

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