Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Vesna, de Serrano"'
Autor:
Vesna de Serrano, Madeline R. Shay, Rania Dumarieh, Matthew K. Thompson, Reza A. Ghiladi, Stefan Franzen
Publikováno v:
Journal of Porphyrins and Phthalocyanines. 25:756-771
As multifunctional catalytic hemoglobins, dehaloperoxidase isoenzymes A and B (DHP A and B) are among the most versatile hemoproteins in terms of activities displayed. The ability of DHP to bind over twenty different substrates in the distal pocket m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::01669e845c31bd54448c14bc33f1850c
https://doi.org/10.1142/s1088424621500826
https://doi.org/10.1142/s1088424621500826
Publikováno v:
Journal of Inorganic Biochemistry. 238:112020
Dehaloperoxidase (DHP) from the marine polychaete Amphitrite ornata is a multifunctional enzyme that possesses peroxidase, peroxygenase, oxidase and oxygenase activities. Herein, we investigated the reactivity of DHP B with bisphenol A (BPA) and rela
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a386a407d22c5c94573f06225d73a9aa
https://doi.org/10.1016/j.jinorgbio.2022.112020
https://doi.org/10.1016/j.jinorgbio.2022.112020
Publikováno v:
Journal of inorganic biochemistry. 236
The multifunctional catalytic globin dehaloperoxidase (DHP) from the marine worm Amphitrite ornata was shown to catalyze the H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee0939889b071ad15db10b4dd1a59fb3
https://pubmed.ncbi.nlm.nih.gov/35969974
https://pubmed.ncbi.nlm.nih.gov/35969974
Autor:
Jason C. Hurlbert, Casey Crooks, Franz J. St John, Vesna de Serrano, Elizabeth Bales, Edwin Pozharski, James Kennon Smith, Peter Balogun, Diane M. Dietrich
Publikováno v:
Biochemical Journal
Glycoside hydrolase family 30 subfamily 8 (GH30-8) β-1,4-endoxylanases are known for their appendage-dependent function requiring recognition of an α-1,2-linked glucuronic acid (GlcA) common to glucuronoxylans for hydrolysis. Structural studies hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6929c214f71b15f472fbe9ddbcc2d4b
https://doi.org/10.1042/bcj20180050
https://doi.org/10.1042/bcj20180050
Publikováno v:
Biochemistry
Dehaloperoxidase hemoglobin A (DHP A) is a multifunctional hemoglobin that appears to have evolved oxidative pathways for the degradation of xenobiotics as a protective function that complements the oxygen transport function. DHP A possesses at least
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13caba4dae96b12bee4c0e75fb9b1901
http://europepmc.org/articles/PMC4203366
http://europepmc.org/articles/PMC4203366
Publikováno v:
Archives of Biochemistry and Biophysics. 673:108079
The multifunctional catalytic hemoglobin dehaloperoxidase (DHP) from the terebellid polychaete Amphitrite ornata was found to catalyze the H2O2-dependent oxidation of EPA Priority Pollutants (4-Me-o-cresol, 4-Cl-m-cresol and pentachlorophenol) and EP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b722a22b5d68a341b57a7caff4f5c6b2
https://doi.org/10.1016/j.abb.2019.108079
https://doi.org/10.1016/j.abb.2019.108079
Autor:
Stefan Franzen, Junjie Zhao, Vesna de Serrano, Rania Dumarieh, Matthew K. Thompson, Reza A. Ghiladi
Publikováno v:
The Journal of Physical Chemistry B. 116:12065-12077
The distal histidine mutations of dehaloperoxidase-hemoglobin A (DHP A) to aspartate (H55D) and asparagine (H55N) have been prepared to study the role played by the distal histidine in both activation and protection against oxidation by radicals in h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d90442e649efa1260747c9961428f2ad
https://doi.org/10.1021/jp300014b
https://doi.org/10.1021/jp300014b
Autor:
Matthew K. Thompson, Barry D. Howes, Michael F. Davis, Francesco P. Nicoletti, Vesna de Serrano, Giulietta Smulevich, Stefan Franzen
Publikováno v:
Biophysical Journal. 99:1586-1595
Dehaloperoxidase (DHP) from the annelid Amphitrite ornata is a catalytically active hemoglobin-peroxidase that possesses a unique internal binding cavity in the distal pocket above the heme. The previously published crystal structure of DHP shows 4-i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb3cb39938b3d808d354d46c7e0bb440
https://doi.org/10.1016/j.bpj.2010.05.041
https://doi.org/10.1016/j.bpj.2010.05.041
Publikováno v:
Biophysical Journal. 93:2429-2435
The infrared spectroscopy of elastin-like polypeptides and the relation to the inverse thermal transition are discussed. To correlate the spectroscopic observations with structure a density function theory model was created that captures the essentia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa12846e646646a44331f652f8fc7654
https://doi.org/10.1529/biophysj.106.100594
https://doi.org/10.1529/biophysj.106.100594
Publikováno v:
Structure. 11:747-751
Room temperature crystal structures of crosslinked H-Ras bound to GMPPNP were solved in 50% 2,2,2-trifluoroethanol, 60% 1,6-hexanediol, and 50% isopropanol. The disordered switch II region of Ras is ordered in the presence of 2,2,2-trifluoroethanol o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0daef8e20ce72e7f310053cb46314adf
https://doi.org/10.1016/s0969-2126(03)00128-x
https://doi.org/10.1016/s0969-2126(03)00128-x