Detalhe da pesquisa
1.
Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine.
Biochemistry
; 62(3): 835-850, 2023 02 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-36706455
2.
The staphylococcal inhibitory protein SPIN binds to human myeloperoxidase with picomolar affinity but only dampens halide oxidation.
J Biol Chem
; 298(11): 102514, 2022 11.
Artigo
em Inglês
| MEDLINE | ID: mdl-36150500
3.
Glycosylation site Asn168 is important for slow in vivo clearance of recombinant human diamine oxidase heparin-binding motif mutants.
Glycobiology
; 32(5): 404-413, 2022 04 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-35088086
4.
Reaction intermediate rotation during the decarboxylation of coproheme to heme b in C. diphtheriae.
Biophys J
; 120(17): 3600-3614, 2021 09 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-34339636
5.
Arresting the Catalytic Arginine in Chlorite Dismutases: Impact on Heme Coordination, Thermal Stability, and Catalysis.
Biochemistry
; 60(8): 621-634, 2021 03 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-33586945
6.
X-ray-induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner.
J Biol Chem
; 295(39): 13488-13501, 2020 09 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-32723869
7.
Reaction of human peroxidasin 1 compound I and compound II with one-electron donors.
Arch Biochem Biophys
; 681: 108267, 2020 03 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-31953133
8.
The leucine-rich repeat domain of human peroxidasin 1 promotes binding to laminin in basement membranes.
Arch Biochem Biophys
; 689: 108443, 2020 08 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-32485152
9.
Roles of distal aspartate and arginine of B-class dye-decolorizing peroxidase in heterolytic hydrogen peroxide cleavage.
J Biol Chem
; 293(38): 14823-14838, 2018 09 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-30072383
10.
Insights into the Active Site of Coproheme Decarboxylase from Listeria monocytogenes.
Biochemistry
; 57(13): 2044-2057, 2018 04 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-29536725
11.
Pre-steady-state Kinetics Reveal the Substrate Specificity and Mechanism of Halide Oxidation of Truncated Human Peroxidasin 1.
J Biol Chem
; 292(11): 4583-4592, 2017 03 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-28154175
12.
Structure of human promyeloperoxidase (proMPO) and the role of the propeptide in processing and maturation.
J Biol Chem
; 292(20): 8244-8261, 2017 05 19.
Artigo
em Inglês
| MEDLINE | ID: mdl-28348079
13.
Coproheme decarboxylases - Phylogenetic prediction versus biochemical experiments.
Arch Biochem Biophys
; 640: 27-36, 2018 02 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-29331688
14.
Posttranslational modification of heme in peroxidases - Impact on structure and catalysis.
Arch Biochem Biophys
; 643: 14-23, 2018 04 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-29462588
15.
Posttranslational Modification of Heme b in a Bacterial Peroxidase: The Role of Heme to Protein Ester Bonds in Ligand Binding and Catalysis.
Biochemistry
; 56(34): 4525-4538, 2017 08 29.
Artigo
em Inglês
| MEDLINE | ID: mdl-28762722
16.
Reaction intermediate rotation during the decarboxylation of coproheme to heme b in C. diphtheriae.
Biophys J
; 120(21): 4903, 2021 Nov 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-34624219
17.
Chemistry and Molecular Dynamics Simulations of Heme b-HemQ and Coproheme-HemQ.
Biochemistry
; 55(38): 5398-412, 2016 09 27.
Artigo
em Inglês
| MEDLINE | ID: mdl-27599156
18.
Introduction of germline residues improves the stability of anti-HIV mAb 2G12-IgM.
Biochim Biophys Acta
; 1854(10 Pt A): 1536-44, 2015 Oct.
Artigo
em Inglês
| MEDLINE | ID: mdl-25748881
19.
Dimeric chlorite dismutase from the nitrogen-fixing cyanobacterium Cyanothece sp. PCC7425.
Mol Microbiol
; 96(5): 1053-68, 2015 Jun.
Artigo
em Inglês
| MEDLINE | ID: mdl-25732258
20.
Eukaryotic Catalase-Peroxidase: The Role of the Trp-Tyr-Met Adduct in Protein Stability, Substrate Accessibility, and Catalysis of Hydrogen Peroxide Dismutation.
Biochemistry
; 54(35): 5425-38, 2015 Sep 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-26290940