Vesna Sator de Serrano

Works (14)

Updated: April 25th, 2025 17:30

2024 article

Structural Comparison of Substrate Binding Sites in Dehaloperoxidase A and B

Aktar, M. S., Serrano, V., Ghiladi, R. A., & Franzen, S. (2024, July 3). Biochemistry, Vol. 63, pp. 1761–1773.

By: M. Aktar n, V. Serrano n, R. Ghiladi n  & S. Franzen n 

MeSH headings : Crystallography, X-Ray; Substrate Specificity; Binding Sites; Peroxidases / chemistry; Peroxidases / metabolism; Catalytic Domain; Models, Molecular; Protein Conformation; Animals; Kinetics
topics (OpenAlex): Heme Oxygenase-1 and Carbon Monoxide; Hemoglobin structure and function; Metal-Catalyzed Oxygenation Mechanisms
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Sources: Web Of Science, NC State University Libraries
Added: July 22, 2024

2021 article

A new inhibition mechanism in the multifunctional catalytic hemoglobin dehaloperoxidase as revealed by the DHP A(V59W) mutant: A spectroscopic and crystallographic study

Thompson, M. K., Shay, M. R., Serrano, V., Dumarieh, R., Ghiladi, R. A., & Franzen, S. (2021, June 22). Journal of Porphyrins and Phthalocyanines, Vol. 7.

By: M. Thompson *, M. Shay *, V. Serrano n, R. Dumarieh n, R. Ghiladi n  & S. Franzen n 

author keywords: Peroxidase; hemoglobin; structure-function; tryptophan; inhibition
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Neonatal Health and Biochemistry
TL;DR: The data reveal a new mechanism of DHP inhibition, namely a shift towards a non-reactive form by OH that is strongly stabilized (presumably through H-bonding interactions) by the presence of W59 in the distal cavity. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 23, 2021

2014 article

A Model for the Flexibility of the Distal Histidine in Dehaloperoxidase-Hemoglobin A Based on X-ray Crystal Structures of the Carbon Monoxide Adduct

Zhao, J., Serrano, V., & Franzen, S. (2014, March 27). Biochemistry, Vol. 53, pp. 2474–2482.

By: J. Zhao n, V. Serrano n & S. Franzen n 

MeSH headings : Amino Acid Sequence; Carbon Monoxide / chemistry; Crystallography, X-Ray; Electrophoresis, Polyacrylamide Gel; Hemoglobin A / chemistry; Hemoglobins / chemistry; Histidine / chemistry; Molecular Sequence Data; Peroxidases / chemistry; Protein Conformation
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Neonatal Health and Biochemistry
TL;DR: The X-ray crystallographic structure of the carbonmonoxy complex (DHPCO) is reported, supporting the modified hypothesis suggesting a competition between the strength of interactions with heme ligand and the heme propionates as the factors that determine the conformation of the distal 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

2013 article

Structural and Kinetic Study of an Internal Substrate Binding Site in Dehaloperoxidase-Hemoglobin A from Amphitrite ornata

Zhao, J., Serrano, V., Zhao, J., Le, P., & Franzen, S. (2013, March 12). Biochemistry, Vol. 52, pp. 2427–2439.

By: J. Zhao n, V. Serrano n, J. Zhao n, P. Le n & S. Franzen n 

MeSH headings : 2-Propanol / chemistry; Animals; Crystallography, X-Ray; Dimethyl Sulfoxide / chemistry; Hemoglobins / chemistry; Hemoglobins / metabolism; Kinetics; Methanol / chemistry; Models, Molecular; Peroxidases / chemistry; Peroxidases / metabolism; Phenols / chemistry; Polychaeta / chemistry; Polychaeta / enzymology; Polychaeta / metabolism; Protein Conformation
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Erythrocyte Function and Pathophysiology
TL;DR: The X-ray crystal structure is consistent with the presence of an internal active site above the heme α-edge, in which the substrate would be oxidized in two consecutive steps inside the enzyme, followed by attack by H2O via a water channel in the protein. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2012 journal article

The Role of the Distal Histidine in H2O2 Activation and Heme Protection in both Peroxidase and Globin Functions

The Journal of Physical Chemistry B, 116(40), 12065–12077.

By: J. Zhao n, V. de Serrano n, R. Dumarieh n, M. Thompson n, R. Ghiladi n  & S. Franzen n 

Contributors: J. Zhao n, V. De Serrano n, R. Dumarieh n, M. Thompson n, R. Ghiladi n  & S. Franzen n 

MeSH headings : Biocatalysis; Chlorophenols / chemistry; Chlorophenols / metabolism; Heme / chemistry; Heme / metabolism; Hemoglobin A / chemistry; Hemoglobin A / metabolism; Histidine / chemistry; Histidine / genetics; Histidine / metabolism; Hydrogen Peroxide / chemistry; Hydrogen Peroxide / metabolism; Models, Molecular; Molecular Structure; Mutation; Oxidation-Reduction; Peroxidases / chemistry; Peroxidases / metabolism; Quinones / chemistry; Quinones / metabolism
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Porphyrin Metabolism and Disorders
TL;DR: The distal histidine mutations of dehaloperoxidase-hemoglobin A to aspartate (H55D) and asparagine and H55N have been prepared to study the role played by the distal Histidine in both activation and protection against oxidation by radicals in heme proteins. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries, ORCID, Crossref
Added: August 6, 2018

2011 journal article

Functional Consequences of the Creation of an Asp-His-Fe Triad in a 3/3 Globin

Biochemistry, 50(44), 9664–9680.

By: E. D’Antonio n, J. D’Antonio n, V. de Serrano n, H. Gracz n, M. Thompson n, R. Ghiladi n , E. Bowden n , S. Franzen n 

Contributors: E. Dantonio n, J. Dantonio n, V. De Serrano n, H. Gracz n, M. Thompson n, R. Ghiladi n , E. Bowden n , S. Franzen n 

MeSH headings : Animals; Aspartic Acid / chemistry; Aspartic Acid / genetics; Catalytic Domain / genetics; Crystallography, X-Ray; Electrochemistry; Globins / chemistry; Globins / genetics; Helminth Proteins / chemistry; Helminth Proteins / genetics; Histidine / chemistry; Histidine / genetics; Magnetic Resonance Spectroscopy; Mutagenesis, Site-Directed; Polychaeta / enzymology; Polychaeta / genetics; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman
topics (OpenAlex): Hemoglobin structure and function; Metalloenzymes and iron-sulfur proteins; Enzyme Structure and Function
TL;DR: The results suggest that the proximal charge relay in peroxidases regulate the redox potential of the heme Fe but that the trans effect is a carefully balanced property that can both activate H( 2)O(2) and attract ligation by the distal histidine. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries, ORCID, Crossref
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)
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6. Clean Water and Sanitation (OpenAlex)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2010 journal article

Structure of dehaloperoxidase B at 1.58 angstrom resolution and structural characterization of the AB dimer from Amphitrite ornata

Acta Crystallographica. Section D, Biological Crystallography, 66, 529–538.

By: V. Serrano, J. D'Antonio, S. Franzen  & R. Ghiladi 

Source: 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)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2008 article

Distal histidine conformational flexibility in dehaloperoxidase fromAmphitrite ornata

Chen, Z., Serrano, V., Betts, L., & Franzen, S. (2008, December 17). Acta Crystallographica Section D Biological Crystallography, Vol. 65, pp. 34–40.

By: Z. Chen n, V. Serrano n, L. Betts * & S. Franzen n 

MeSH headings : Animals; Crystallization; Crystallography, X-Ray; Heme Oxygenase (Decyclizing) / chemistry; Heme Oxygenase (Decyclizing) / metabolism; Hemoglobins / chemistry; Hemoglobins / metabolism; Histidine / chemistry; Histidine / metabolism; Iodobenzenes / chemistry; Iodobenzenes / metabolism; Peroxidases / chemistry; Peroxidases / metabolism; Polychaeta / enzymology; Protein Binding; Protein Conformation; Solvents
topics (OpenAlex): Hemoglobin structure and function; Heme Oxygenase-1 and Carbon Monoxide; Erythrocyte Function and Pathophysiology
TL;DR: It is reported that the distal histidine, His55, exhibits conformational flexibility in the deoxy form and is consequently observed in two solvent-exposed conformations more than 9.5 A away from the heme, analogous to the open conformation of sperm whale myoglobin. (via Semantic Scholar)
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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)
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Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018

2004 article

Crystal Structures of Ral-GppNHp and Ral-GDP Reveal Two Binding Sites that Are Also Present in Ras and Rap

Nicely, N. I., Kosak, J., Serrano, V., & Mattos, C. (2004, November 1). Structure.

By: N. Nicely n, J. Kosak n, V. Serrano n & C. Mattos n

MeSH headings : Amino Acid Sequence; Binding Sites; Catalytic Domain; Crystallography, X-Ray; Guanosine Diphosphate / chemistry; Guanosine Diphosphate / metabolism; Guanosine Triphosphate / analogs & derivatives; Guanosine Triphosphate / chemistry; Guanosine Triphosphate / metabolism; Models, Molecular; Molecular Sequence Data; Protein Conformation; Sequence Homology, Amino Acid; rap GTP-Binding Proteins / chemistry; rap GTP-Binding Proteins / metabolism; ras Proteins / chemistry; ras Proteins / metabolism
topics (OpenAlex): Protein Kinase Regulation and GTPase Signaling; Enzyme Structure and Function; RNA and protein synthesis mechanisms
TL;DR: Clustering of conserved residues on the surface of Ral-GppNHp identifies two putative sites for protein-protein interaction, one of which is adjacent to switch I and the other is modulated by switch II and is obstructed in RAl-GDP. (via Semantic Scholar)
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8. Decent Work and Economic Growth (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

2003 article

Organic Solvents Order the Dynamic Switch II in Ras Crystals

Buhrman, G., Serrano, V., & Mattos, C. (2003, July 1). Structure.

By: G. Buhrman n, V. Serrano n & C. Mattos n

MeSH headings : Crystallization; Guanosine Triphosphate / analogs & derivatives; Guanosine Triphosphate / chemistry; Organic Chemicals / chemistry; Solvents / chemistry; ras Proteins / chemistry
topics (OpenAlex): Protein Kinase Regulation and GTPase Signaling; Enzyme Structure and Function; Protein Structure and Dynamics
TL;DR: The results suggest that hydrophobic solvents can be used in general to order short biologically relevant segments of disordered regions in protein crystals by favoring H-bonding interactions between atoms that are highly solvated and mobile in aqueous solution. (via Semantic Scholar)
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6. Clean Water and Sanitation (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

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