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.
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)
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: 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.
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
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.
Source: NC State University Libraries
Added: August 6, 2018
2012 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.
Contributors: S. Franzen* , 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)
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
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, 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
2009 journal article
Characterization of Dehaloperoxidase Compound ES and Its Reactivity with Trihalophenols†
Biochemistry, 48(5), 995–1005.
Contributors: J. Feducia n , 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)
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
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