Results 11 to 20 of about 1,942 (200)

Light‐Induced Pulsed EPR Dipolar Spectroscopy on a Paradigmatic Hemeprotein

open access: yesChemPhysChem, 2019
Light‐induced pulsed EPR dipolar spectroscopic methods allow the determination of nanometer distances between paramagnetic sites. Here we employ orthogonal spin labels, a chromophore triplet state and a stable radical, to carry out distance measurements ...
Maria Giulia Dal Farra   +8 more
semanticscholar   +6 more sources

Evolutionary Pro-To-Thr Mutation in the Intrinsically Disordered Domain of ANP32 Family Members Modulates Their Target Binding Modes [PDF]

open access: yesAdvanced Science, Volume 12, Issue 12, March 27, 2025.
Gene duplication has allowed protein evolution toward novel functions and mechanisms. The differences between paralogous genes frequently rely on the sequence of disordered regions.
Baños-Jaime, Blanca   +8 more
core   +2 more sources

Implication to the catalytic process of hemeproteins [PDF]

open access: bronzeActa Crystallographica Section A Foundations of Crystallography, 2011
Y. Ohgo   +8 more
openalex   +3 more sources

How does NO activate hemeproteins? [PDF]

open access: bronzeFEBS Letters, 1994
NO was reported to activate guanylate cyclase and, recently, prostaglandin H synthase. NO interaction with the heme component in different hemeproteins is determined by ligand property, electronic configuration of the heme iron and the specific effects contributed by the protein structure.
Ah‐Lim Tsai
openalex   +5 more sources

Biomimetic chemistry of hemeproteins.

open access: bronzeThe Keio Journal of Medicine, 1989
Hemeproteins play important physiological roles for an oxygen metabolism in living organisms. Their functions are divided to three main groups, i) hemoglobins, myoglobins and the cytochromes which function by transporting and storing dioxygen and electrons; ii) catalase and peroxidases which are activated by hydrogen peroxide, iii) cytochrome oxidase ...
David Dolphin
openalex   +5 more sources

Mechanism of Sulfide Binding by Ferric Hemeproteins [PDF]

open access: greenInorganic Chemistry, 2018
The reaction of hydrogen sulfide (H2S) with hemeproteins is a key physiological reaction; still, its mechanism and implications are not completely understood. In this work, we propose a combination of experimental and theoretical tools to shed light on the reaction in model system microperoxidase 11 (MP11-FeIII) and myoglobin (Mb-FeIII), from the ...
Fernando M. Boubeta   +5 more
openalex   +5 more sources

Recombinant Hemoglobin II From Lucina pectinata: A Large-Scale Method For Hemeprotein Expression in E. coli

open access: greenThe Protein Journal, 2010
Cacimar Ramos   +6 more
openalex   +3 more sources

Behind the Optimization of the Sensor Film: Bioconjugation of Triangular Gold Nanoparticles with Hemoproteins for Sensitivity Enhancement of Enzymatic Biosensors

open access: yesBiosensors, 2023
Electrochemical biosensors are widely used in a multitude of applications, such as medical, nutrition, research, among other fields. These sensors have been historically used and have not undergone many changes in terms of the involved electrochemical ...
Miriam Chávez   +6 more
doaj   +1 more source

Hsp90 in Human Diseases: Molecular Mechanisms to Therapeutic Approaches

open access: yesCells, 2022
The maturation of hemeprotein dictates that they incorporate heme and become active, but knowledge of this essential cellular process remains incomplete. Studies on chaperon Hsp90 has revealed that it drives functional heme maturation of inducible nitric
Mamta P. Sumi, Arnab Ghosh
doaj   +1 more source

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