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Works (13)
Updated: April 5th, 2024 03:12
2021 journal article
A new inhibition mechanism in the multifunctional catalytic hemoglobin dehaloperoxidase as revealed by the DHP A(V59W) mutant: A spectroscopic and crystallographic study
JOURNAL OF PORPHYRINS AND PHTHALOCYANINES, 25(7-8), 756–771.
author keywords: Peroxidase; hemoglobin; structure-function; tryptophan; inhibition
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Sources: Web Of Science, NC State University Libraries
Added: August 23, 2021
2014 journal 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
BIOCHEMISTRY, 53(15), 2474–2482.
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
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)
doi.org (publisher)
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
2013 journal article
Structural and Kinetic Study of an Internal Substrate Binding Site in Dehaloperoxidase-Hemoglobin A from Amphitrite ornata
BIOCHEMISTRY, 52(14), 2427–2439.
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
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)
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
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.
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
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
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.
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
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Sources: Web Of Science, NC State University Libraries, ORCID, Crossref
Added: August 6, 2018
2010 journal article
Internal Binding of Halogenated Phenols in Dehaloperoxidase-Hemoglobin Inhibits Peroxidase Function
BIOPHYSICAL JOURNAL, 99(5), 1586–1595.
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
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 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
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.
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.
Source: NC State University Libraries
Added: August 6, 2018
2009 journal article
Different Modes of Binding of Mono-, Di-, and Trihalogenated Phenols to the Hemoglobin Dehaloperoxidase from Amphitrite ornata
BIOCHEMISTRY, 48(10), 2164–2172.
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
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 Goal Categories
3. Good Health and Well-being
(Web of Science)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018
2009 journal article
Distal histidine conformational flexibility in dehaloperoxidase from Amphitrite ornata
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 65, 34–40.
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
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)
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
2007 journal article
X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned from Amphitrite ornata
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 63, 1094–1101.
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
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 Goal Categories
3. Good Health and Well-being
(Web of Science)
Sources: Web Of Science, NC State University Libraries
Added: August 6, 2018
2004 journal article
Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap
STRUCTURE, 12(11), 2025–2036.
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
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
8. Decent Work and Economic Growth
(OpenAlex)
Source: Web Of Science
Added: August 6, 2018
2003 journal article
Organic solvents order the dynamic switch II in Ras crystals
STRUCTURE, 11(7), 747–751.
MeSH headings : Crystallization; Guanosine Triphosphate / analogs & derivatives; Guanosine Triphosphate / chemistry; Organic Chemicals / chemistry; Solvents / chemistry; ras Proteins / chemistry
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)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
6. Clean Water and Sanitation
(OpenAlex)
Source: Web Of Science
Added: August 6, 2018
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