Rania Dumarieh

Works (6)

Updated: July 5th, 2023 15:50

2022 journal article

Mossbauer studies of the ferryl, ferrous and ferric states of dehaloperoxidase from A. ornata

JOURNAL OF INORGANIC BIOCHEMISTRY, 234.

By: C. Popescu *, T. Dinh *, H. Chen *, D. Miller*, A. Washburn*, A. McGuire  n, R. Dumarieh n, J. D'Antonio n, R. Ghiladi n 

author keywords: Mossbauer spectroscopy; Peroxidase; Heme enzyme; Ferryl; Globin
MeSH headings : Animals; Ferric Compounds / chemistry; Heme / chemistry; Hemoglobins / chemistry; Hydrogen Peroxide / chemistry; Iron / chemistry; Myoglobin / chemistry; Peroxidases / metabolism; Polychaeta; Spectroscopy, Mossbauer
TL;DR: The isomer shift and quadrupole splitting of DHP in the four states studied are expectedly similar to both peroxidases and to myoglobin, and differences in electronic structure between DHP and other heme proteins and enzyme are observed in the high-field Mössbauer spectra of the ferric state, which show pH-dependent zero-field splittings suggesting a heme site in which the ligand field strength at the iron ion is tuned by pH. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries
Added: December 12, 2022

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.

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
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

2013 journal article

Tyrosyl radicals in dehaloperoxidase how nature deals with evolving an oxygen-binding globin to a biologically relevant peroxidase

Journal of Biological Chemistry, 288(46), 33470–33482.

By: R. Dumarieh, J. D'Antonio, A. Deliz-Liang, T. Smirnova , D. Svistunenko & R. Ghiladi 

Source: 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
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

Nonphotochemical Base-Catalyzed Hydroxylation of 2,6-Dichloroquinone by H2O2Occurs by a Radical Mechanism

The Journal of Physical Chemistry B, 116(5), 1666–1676.

By: S. Franzen n , K. Sasan, B. Sturgeon*, B. Lyon*, B. Battenburg*, H. Gracz*, R. Dumariah, R. Ghiladi* 

Contributors: S. Franzen n , K. Sasan, B. Sturgeon*, B. Lyon*, B. Battenburg*, H. Gracz*, R. Dumariah, R. Ghiladi* 

MeSH headings : Animals; Benzoquinones / chemistry; Benzoquinones / metabolism; Catalysis; Chlorophenols / metabolism; Hydrogen Peroxide / metabolism; Peroxidases / metabolism; Polychaeta / enzymology; Polychaeta / metabolism
TL;DR: The control experiments and precedents in studies of other peroxidases lead to the conclusion that hydroxylation will be observed following any process that leads to the formation of the 2,6-DCQ at pH > 7, regardless of the catalyst used in the2,4, 6-TCP oxidation reaction. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries, ORCID, Crossref
Added: August 6, 2018

2009 journal article

Characterization of Dehaloperoxidase Compound ES and Its Reactivity with Trihalophenols†

Biochemistry, 48(5), 995–1005.

By: J. Feducia n , R. Dumarieh n, L. Gilvey n, T. Smirnova n , S. Franzen n  & R. Ghiladi n 

Contributors: J. Feducia n , R. Dumarieh n, L. Gilvey n, T. Smirnova n , S. Franzen n  & R. Ghiladi n 

MeSH headings : Animals; Binding Sites; Chlorophenols / chemistry; Chlorophenols / metabolism; Crystallography, X-Ray; Cytochrome-c Peroxidase / chemistry; Cytochrome-c Peroxidase / metabolism; Electron Transport Complex IV / chemistry; Electron Transport Complex IV / metabolism; Hemoglobins / chemistry; Hemoglobins / metabolism; Peroxidases / chemistry; Peroxidases / metabolism; Polychaeta / enzymology
TL;DR: It is demonstrated that the first detectable intermediate following the addition of hydrogen peroxide to ferric DHP contains both a ferryl heme and a tyrosyl radical, analogous to Compound ES of cytochrome c peroxidase. (via Semantic Scholar)
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Sources: Web Of Science, NC State University Libraries, ORCID, Crossref
Added: August 6, 2018

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