Results 11 to 20 of about 2,121 (177)
Mechanism of Sulfide Binding by Ferric Hemeproteins [PDF]
Inorganic 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
openaire +4 more sources
In Silico Insight into the Reductive Nitrosylation of Ferric Hemeproteins
Inorganic Chemistry, 2020 A combination of in silico methods was used to extend the experimental description of the reductive nitrosylation mechanism in ferric hemeproteins with the molecular details of the role of surrounding amino acids. The computational strategy consisted in the estimation of potential energy profiles for the transition process associated with the ...
Nicolás O. Foglia +2 more
core +6 more sources
Optimization of Hnox Protein Production in Escherichia Coli
Cumhuriyet Science Journal, 2017 Hemeproteinscarry a variety of different functions in organisms ranging from steroidbiosynthesis to respiration, signaling to drug metabolism. In industry,hemeproteins are used for production of drugs such as: pravastatin for loweringcholesterol ...
Nur Başak Sürmeli
doaj +3 more sources
A quantitative model for oxygen uptake and release in a family of hemeproteins [PDF]
Bioinformatics, 2016 Abstract Motivation: Hemeproteins have many diverse functions that largely depend on the rate at which they uptake or release small ligands, like oxygen. These proteins have been extensively studied using either simulations or experiments, albeit only qualitatively and one or two proteins at a time.
Juan P. Bustamante +5 more
openaire +5 more sources
Biomimetic chemistry of hemeproteins.
The 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
openaire +4 more sources
Mechanistics of pH-Dependent Sulfmyoglobin Formation: Spin Control and His64 Proton Relay
Journal of ChemistryThe chemistry of hydrogen sulfide (H2S) has been directed towards physiologically relevant hemeproteins, including myoglobin, hemoglobin, and other similar proteins.
Angel D. Rodriguez-Mackenzie +4 more
doaj +2 more sources
OXIDATION‐REDUCTION REACTIONS OF HEMEPROTEINS
Annals of the New York Academy of Sciences, 1975 iiiii Then on past C 1, C, and A On through copper and all the way To oxygen, with two‐faced grin Cavorting and contorting with unpaired spin ...
C E, Castro +5 more
openaire +3 more sources
, 2007 Hemeproteins are widespread in all groups of living organisms, both as components of key biological processes as well as in very specific metabolic pathways. By variation of either the heme porphyrin structure or the heme protein environment, the function and behavior of the hemeproteins may vary drastically, allowing its role in the most diverse ...
Inês A. C. Pereira +2 more
openaire +2 more sources
Vibrational Energy Flow in Hemeproteins
19th International Conference on Ultrafast Phenomena, 2014 We demonstrate that time-resolved anti-Stokes ultraviolet resonance Raman spectroscopy is a powerful tool for studying the vibrational energy flow in proteins with a spatial resolution of a single amino acid residue.
Yasuhisa Mizutani +4 more
core +3 more sources
Hemeproteins: Recent Advances in Quantitative XANES Analysis
AIP Conference Proceedings, 2007 Recently, we have shown that multiple scattering (MS) theory, via the MXAN package, is able to reproduce the experimental X‐ray absorption near edge structure (XANES) data of biological samples, in particular hemeproteins, from the rising edge up to ∼150–200 eV above the edge.
A. ARCOVITO +3 more
openaire +2 more sources