Works (8)
Updated: July 11th, 2023 20:10
2007 journal article
Probing protein adsorption onto mercaptoundecanoic acid stabilized gold nanoparticles and surfaces by quartz crystal microbalance and zeta-potential measurements
LANGMUIR, 23(11), 6053–6062.
MeSH headings : Adsorption; Animals; Biosensing Techniques; Cattle; Coated Materials, Biocompatible / chemistry; Cytochromes c / chemistry; Electrochemistry; Fatty Acids / chemistry; Gold / chemistry; Hydrogen-Ion Concentration; In Vitro Techniques; Metal Nanoparticles / chemistry; Myoglobin / chemistry; Proteins / chemistry; Quartz; Serum Albumin, Bovine / chemistry; Surface Properties
TL;DR:
The observation of stable BSA complexes on MUA/AuNPs at the isoelectric point by zeta-potential measurements demonstrates that BSA can sterically stabilize MUA /AuNP.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018
2006 journal article
Hydrophobic distal pocket affects NO-heme geminate recombination dynamics in dehaloperoxidase and H64V myoglobin
JOURNAL OF PHYSICAL CHEMISTRY B, 110(29), 14483–14493.
MeSH headings : Amino Acid Substitution; Animals; Heme / chemistry; Hemoglobins / chemistry; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Kinetics; Models, Chemical; Myoglobin / chemistry; Nitric Oxide / chemistry; Peroxidases / chemistry; Polychaeta / enzymology; Protein Conformation; Time Factors
TL;DR:
A comparison between the more rapid rate constant of the slow geminate phase in DHP-NO and horse heart myoglobin or sperm whale myoglobin suggests that protein interactions with photolyzed NO are weaker in D HP than in the wild-type MbNOs, consistent with the hydrophobic distal pocket of DHP.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
14. Life Below Water
(OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018
2006 journal article
Proximal cavity, distal histidine, and substrate hydrogen-bonding mutations modulate the activity of Amphitrite ornata dehaloperoxidase
BIOCHEMISTRY, 45(30), 9085–9094.
Contributors: S. Franzen n , n, L. Gilvey n, M. Davis n, C. Chaudhary n, T. Sit n , S. Lommel n
MeSH headings : Animals; Binding Sites / genetics; Hemoglobins; Histidine / chemistry; Histidine / genetics; Hydrogen Bonding; Mutagenesis, Site-Directed; Peroxidases / chemistry; Peroxidases / genetics; Peroxidases / metabolism; Phenylalanine / genetics; Polychaeta / enzymology; Polychaeta / genetics; Substrate Specificity / genetics; Tyrosine / genetics; Valine / genetics
TL;DR:
The role of tyrosine 38 (Y38), which hydrogen bonds to the hydroxyl group of the substrate, was probed and it was suggested that abolishing this hydrogen bond may open a pathway for the escape of the one-electron product, the phenoxy radical leading to polymeric products.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
14. Life Below Water
(OpenAlex)
Sources: Web Of Science, NC State University Libraries, ORCID
Added: August 6, 2018
2006 journal article
Resonance Raman study of ferric heme adducts of dehaloperoxidase from Amphitrite ornata
BIOCHEMISTRY, 45(48), 14275–14284.
MeSH headings : Animals; Heme / chemistry; Heme / metabolism; Hydrogen Bonding; Iron / chemistry; Iron / metabolism; Ligands; Models, Molecular; Molecular Conformation; Peroxidases / chemistry; Peroxidases / metabolism; Polychaeta / enzymology; Porphyrins / chemistry; Spectrum Analysis, Raman
TL;DR:
The Raman data provide the first direct measurement of the effect of axial ligation on the heme iron in DHP, in which a strongly hydrogen-bonded backbone carbonyl (>C=O) polarizes the proximal histidine.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
6. Clean Water and Sanitation
(OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018
2006 journal article
Spectroscopic study of substrate binding to the carbonmonoxy form of dehaloperoxidase from Amphitrite ornata
JOURNAL OF PHYSICAL CHEMISTRY B, 110(26), 13264–13276.
MeSH headings : Animals; Models, Molecular; Peroxidases / chemistry; Peroxidases / metabolism; Polychaeta / enzymology; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Substrate Specificity
TL;DR:
The dynamics of substrate binding in DHP are explored using Fourier transform infrared spectroscopy and flash photolysis to identify a number of discrete conformations at the active site that are involved in promotion of substrate and cosubstrate entry and exit.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
14. Life Below Water
(OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018
2006 journal article
The pH dependence of the activity of dehaloperoxidase from Amphitrite ornata
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1774(1), 121–130.
author keywords: peroxidase; Fourier-transform infrared spectroscopy; X-ray crystallography; enzyme kinetics
MeSH headings : Animals; Crystallography, X-Ray; Hemoglobins / metabolism; Hydrogen-Ion Concentration; Kinetics; Peroxidases / metabolism; Phenols / metabolism; Polychaeta / enzymology; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared
TL;DR:
A study of the pH dependence of the activity of DHP reveals a substantial difference in mechanism, and other known peroxidases, which oxidize substrates at the heme edge are discussed by comparison.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018
2005 journal article
Enzyme function of the globin dehaloperoxidase from Amphitrite ornata is activated by substrate binding
BIOCHEMISTRY, 44(48), 15637–15644.
Contributors: n, L. Gilvey n, M. Davis n, M. Godek n, T. Sit n , S. Lommel n, S. Franzen n
MeSH headings : Animals; Cloning, Molecular; Enzyme Activation; Escherichia coli / enzymology; Escherichia coli / genetics; Globins / metabolism; Hemoglobins; Hydrogen Peroxide / metabolism; Peroxidases / antagonists & inhibitors; Peroxidases / genetics; Peroxidases / metabolism; Phenols / metabolism; Polychaeta / enzymology; Protein Binding; Recombinant Proteins / isolation & purification; Recombinant Proteins / metabolism
TL;DR:
The present study shows that, unlike other known peroxidases, DHP activity requires the addition of substrate, TBP, prior to the cosubstrate, peroxide.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
6. Clean Water and Sanitation
(OpenAlex)
Sources: Web Of Science, NC State University Libraries, ORCID
Added: August 6, 2018
2004 journal article
Covalent attachment of a nickel nitrilotriacetic acid group to a germanium attenuated total reflectance element
LANGMUIR, 20(4), 1184–1188.
TL;DR:
The surface of a germanium internal reflectance element (IRE) was modified to bind 6X-histidine (his)-tagged biomolecules and binding of his-tagged biotin to nickel nitrilotriacetic acid (Ni-NTA) was observed by ATR-FT-IR spectroscopy.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
6. Clean Water and Sanitation
(OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018
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