Jennifer L. Belyea

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.

By: E. Kaufman n, J. Belyea n, M. Johnson n, Z. Nicholson n, J. Ricks n, P. Shah n, M. Bayless n, T. Pettersson  n ...

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)
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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.

By: S. Franzen n , A. Jasaitis n, J. Belyea n, S. Brewer n, R. Casey n, A. MacFarlane  n, R. Stanley  n, M. Vos  n, J. Martin n

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)
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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.

By: S. Franzen n , J. Belyea n, L. Gilvey n, M. Davis n, C. Chaudhary n, T. Sit n , S. Lommel n

Contributors: S. Franzen n , J. Belyea 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)
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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.

By: J. Belyea n, C. Belyea n, S. Lappi n & S. Franzen n 

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)
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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.

By: K. Nienhaus  n, P. Deng n, J. Belyea n, S. Franzen n  & G. Nienhaus  n

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)
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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.

By: S. Franzen n , L. Gilvey n & J. Belyea n

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)
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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.

By: J. Belyea n, L. Gilvey n, M. Davis n, M. Godek n, T. Sit n , S. Lommel n, S. Franzen n 

Contributors: J. Belyea 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)
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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.

By: B. Smith n, S. Lappi n, S. Brewer n, S. Dembowy n, J. Belyea n & S. Franzen n 

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 Goals Color Wheel
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6. Clean Water and Sanitation (OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

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