Michael A Davis

Works (11)

Updated: April 5th, 2024 04:13

2011 article

Dehaloperoxidase-Hemoglobin from Amphitrite ornata Is Primarily a Monomer in Solution

Thompson, M. K., Franzen, S., Davis, M. F., Oliver, R. C., & Krueger, J. K. (2011, March 21). The Journal of Physical Chemistry B, Vol. 115, pp. 4266–4272.

By: M. Thompson n, S. Franzen n , M. Davis n, R. Oliver * & J. Krueger*

MeSH headings : Animals; Crystallography, X-Ray; Dimerization; Hemoglobins / chemistry; Peroxidases / chemistry; Polychaeta / enzymology; Polychaeta / metabolism; Protein Conformation; Scattering, Small Angle; Solutions / chemistry; X-Ray Diffraction
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Porphyrin Metabolism and Disorders
TL;DR: DHP A is primarily monomeric in solution, but with a detectable level of dimer (~10%), under all conditions studied up to a protein concentration of 3.0 mM, which is likely 10-100-fold lower than the K(d) for dimer formation. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2010 article

Internal Binding of Halogenated Phenols in Dehaloperoxidase-Hemoglobin Inhibits Peroxidase Function

Thompson, M. K., Davis, M. F., Serrano, V., Nicoletti, F. P., Howes, B. D., Smulevich, G., & Franzen, S. (2010, September 1). Biophysical Journal, Vol. 99, pp. 1586–1595.

By: M. Thompson n, M. Davis n, V. Serrano n, F. Nicoletti *, B. Howes*, G. Smulevich *, S. Franzen n 

MeSH headings : Animals; Catalytic Domain; Crystallography, X-Ray; Enzyme Inhibitors / chemistry; Enzyme Inhibitors / metabolism; Enzyme Inhibitors / pharmacology; Halogenation; Hemoglobins / chemistry; Hemoglobins / metabolism; Iodobenzenes / chemistry; Iodobenzenes / metabolism; Iodobenzenes / pharmacology; Kinetics; Models, Molecular; Peroxidases / antagonists & inhibitors; Peroxidases / chemistry; Peroxidases / metabolism; Polychaeta / enzymology; Spectrum Analysis, Raman
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Erythrocyte Function and Pathophysiology
TL;DR: It is demonstrated that DHP has a unique two-site competitive binding mechanism in which the internal and external binding sites communicate through two conformations of the distal histidine of the enzyme, resulting in nonclassical competitive inhibition. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2010 journal article

X-ray structure of the metcyano form of dehaloperoxidase from Amphitrite ornata: Evidence for photoreductive dissociation of the iron-cyanide bond

Acta Crystallographica. Section D, Biological Crystallography, 66, 770–782.

By: V. Serrano, M. Davis, J. Gaff, Q. Zhang, Z. Chen, E. D'Antonio, E. Bowden , R. Rose , S. Franzen 

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

2009 article

Different Modes of Binding of Mono-, Di-, and Trihalogenated Phenols to the Hemoglobin Dehaloperoxidase from Amphitrite ornata

Davis, M. F., Gracz, H., Vendeix, F. A. P., Serrano, V., Somasundaram, A., Decatur, S. M., & Franzen, S. (2009, February 19). Biochemistry, Vol. 48, pp. 2164–2172.

By: M. Davis n, H. Gracz n, F. Vendeix n, V. Serrano n, A. Somasundaram n, S. Decatur n, S. Franzen n 

MeSH headings : Animals; Binding Sites / physiology; Catalysis; Catalytic Domain / physiology; Heme / chemistry; Hemoglobins / chemistry; Hemoglobins / genetics; Hemoglobins / metabolism; Hydrocarbons, Halogenated / chemistry; Hydrocarbons, Halogenated / metabolism; Molecular Conformation; Nuclear Magnetic Resonance, Biomolecular; Peroxidases / chemistry; Peroxidases / genetics; Peroxidases / metabolism; Phenols / chemistry; Phenols / metabolism; Polychaeta / enzymology; Polychaeta / genetics; Potassium Cyanide / chemistry; Protein Binding / physiology; Protein Conformation; Recombinant Proteins / chemistry; Recombinant Proteins / genetics; Recombinant Proteins / metabolism; Substrate Specificity
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Erythrocyte Function and Pathophysiology
TL;DR: The most soluble trihalogenated phenol acts as a highly soluble structural analogue to the native substrate 2,4,6-tribromophenol, and to improve the understanding of substrate binding, the most soluble substrate analogues are compared. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2008 article

Conformational Dynamics Associated with Photodissociation of CO from Dehaloperoxidase Studied Using Photoacoustic Calorimetry

Mikšovská, J., Horsa, S., Davis, M. F., & Franzen, S. (2008, October 10). Biochemistry, Vol. 47, pp. 11510–11517.

By: J. Mikšovská  n, S. Horsa n, M. Davis n & S. Franzen n 

MeSH headings : Animals; Calorimetry / methods; Carbon Monoxide / chemistry; Catalytic Domain; Hemoglobins / chemistry; Hemoglobins / metabolism; Hemoglobins / radiation effects; Models, Molecular; Peroxidases / chemistry; Peroxidases / metabolism; Peroxidases / radiation effects; Photochemistry; Polychaeta / enzymology; Protein Conformation; Spectrophotometry; Thermodynamics
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Photosynthetic Processes and Mechanisms
TL;DR: The dynamics and energetics of conformational changes observed for dissociation of a ligand from DHP differ significantly from those measured previously for photodissociation of CO from the structural homologue myoglobin, suggesting that structural dynamics in DHP are fine-tuned to enhance the peroxidase function of this protein. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2008 article

Determinants of Substrate Internalization in the Distal Pocket of Dehaloperoxidase Hemoglobin of Amphitrite ornata

Nienhaus, K., Nickel, E., Davis, M. F., Franzen, S., & Nienhaus, G. U. (2008, November 12). Biochemistry, Vol. 47, pp. 12985–12994.

By: K. Nienhaus  n, E. Nickel n, M. Davis n, S. Franzen n  & G. Nienhaus  n

MeSH headings : Animals; Binding Sites; Crystallography, X-Ray; Hemoglobins / chemistry; Hemoglobins / metabolism; Hydrogen-Ion Concentration; Ligands; Peroxidases / chemistry; Peroxidases / metabolism; Polychaeta / enzymology; Protein Conformation; Spectroscopy, Fourier Transform Infrared; Substrate Specificity
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Erythrocyte Function and Pathophysiology
TL;DR: The results on wild-type DHP and its variants indicate that halophenols and a diatomic ligand can indeed simultaneously be present in the distal pocket if thedistal histidine is in the low-pH conformation, in which its side chain is swung out of the Distal pocket. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2008 article

Substrate Binding Triggers a Switch in the Iron Coordination in Dehaloperoxidase from Amphitrite ornata:  HYSCORE Experiments

Smirnova, T. I., Weber, R. T., Davis, M. F., & Franzen, S. (2008, January 25). Journal of the American Chemical Society, Vol. 130, p. 2128-.

By: T. Smirnova n , R. Weber n, M. Davis n & S. Franzen n 

MeSH headings : Animals; Electron Spin Resonance Spectroscopy; Ferric Compounds / chemistry; Ferric Compounds / metabolism; Heme / chemistry; Heme / metabolism; Hemoglobins / chemistry; Hemoglobins / metabolism; Iron / chemistry; Iron / metabolism; Models, Molecular; Peroxidases / chemistry; Peroxidases / metabolism; Polychaeta / enzymology; Protein Binding; Spectrum Analysis / methods; Water / chemistry; Water / metabolism
topics (OpenAlex): Hemoglobin structure and function; Photosynthetic Processes and Mechanisms; Spectroscopy and Quantum Chemical Studies
TL;DR: Continuous wave EPR spectra show that heme iron of DHP at pH 6.0 exists in the high spin state, consistent with a water molecule being the sixth ligand in the iron coordination, and highlights the proposed role of the substrate as a trigger for the switch from hemoglobin to peroxidase. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2007 article

X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned fromAmphitrite ornata

Serrano, V., Chen, Z., Davis, M. F., & Franzen, S. (2007, September 19). Acta Crystallographica Section D Biological Crystallography, Vol. 63, pp. 1094–1101.

By: V. Serrano n, Z. Chen n, M. Davis n & S. Franzen n 

MeSH headings : Animals; Binding Sites; Crystallography, X-Ray / methods; Cysteine / chemistry; Escherichia coli / metabolism; Heme / chemistry; Hemoglobins / chemistry; Hydrogen Bonding; Models, Chemical; Models, Molecular; Molecular Conformation; Peroxidases / chemistry; Polychaeta / metabolism; Protein Conformation; Recombinant Proteins / chemistry; Serine / chemistry
topics (OpenAlex): Hemoglobin structure and function; Porphyrin Metabolism and Disorders; Heme Oxygenase-1 and Carbon Monoxide
TL;DR: Hydrogen-bonding interaction between His55 and the bound diatomic oxygen molecule provides new insight into the catalytic activation of H(2)O(2), which is essential for peroxidase activity. (via Semantic Scholar)
UN Sustainable Development Goals Color Wheel
UN Sustainable Development Goal Categories
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2006 article

Proximal Cavity, Distal Histidine, and Substrate Hydrogen-Bonding Mutations Modulate the Activity of Amphitrite ornata Dehaloperoxidase

Franzen, S., Belyea, J., Gilvey, L. B., Davis, M. F., Chaudhary, C. E., Sit, T. L., & Lommel, S. A. (2006, July 7). Biochemistry, Vol. 45, pp. 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
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Erythrocyte Function and Pathophysiology
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 Goals Color Wheel
UN Sustainable Development Goal Categories
14. Life Below Water (OpenAlex)
Sources: Web Of Science, NC State University Libraries, ORCID
Added: August 6, 2018

2005 article

Enzyme Function of the Globin Dehaloperoxidase from Amphitrite ornata Is Activated by Substrate Binding

Belyea, J., Gilvey, L. B., Davis, M. F., Godek, M., Sit, T. L., Lommel, S. A., & Franzen, S. (2005, November 9). Biochemistry, Vol. 44, pp. 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
topics (OpenAlex): Hemoglobin structure and function; Porphyrin Metabolism and Disorders; Heme Oxygenase-1 and Carbon Monoxide
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 Goals Color Wheel
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation (OpenAlex)
Sources: Web Of Science, NC State University Libraries, ORCID
Added: August 6, 2018

1998 conference paper

A study of the molecular interactions occurring in blends of cellulose esters and phenolic polymers

In T. J. Heinze & W. G. Glasser (Eds.), ACS Symposium Series 688, Cellulose Derivatives (p. 283).

By: M. Davis, X. Wang, M. Myers, J. Iwamiya & S. Kelley 

Ed(s): . T. J. Heinze & W. Glasser

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

Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.

Certain data included herein are derived from the Web of Science© and InCites© (2026) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.