Results 61 to 70 of about 2,605 (236)

Mechanism of Sulfide Binding by Ferric Hemeproteins

open access: yesInorganic 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   +3 more sources

Cloning, Expression, and Purification of a Nitric Oxide Synthase-Like Protein from Bacillus cereus

open access: yesBiochemistry Research International, 2010
The nitric oxide synthase-like protein from Bacillus cereus (bcNOS) has been cloned, expressed, and characterized. This small hemeprotein (356 amino acids in length) has a mass of 43 kDa and forms a dimer.
Heather J. Montgomery   +3 more
doaj   +1 more source

Optimization of Hnox Protein Production in Escherichia Coli

open access: yesCumhuriyet 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   +1 more source

Evaluation of hemolysis effect on hemoglobin measurement by capillary electrophoresis

open access: yesJournal of Analytical Science and Technology, 2019
Background Hemoglobin (Hb) is a hemeprotein with two linked pairs of globin chains. Each chain is connected to a heme residue in its center. Hemoglobinopathies are divided into quantitative and qualitative defects in globin synthesis.
Armin Mokhtariye   +4 more
doaj   +1 more source

Myeloperoxidase can differentiate between sepsis and non-infectious SIRS and predicts mortality in intensive care patients with SIRS

open access: yesIntensive Care Medicine Experimental, 2017
Background Systemic inflammatory response syndrome (SIRS) is a clinical syndrome following inflammation. Clinically, it is difficult to distinguish SIRS following an infection, i.e., sepsis, from non-infectious SIRS.
Irene T. Schrijver   +4 more
doaj   +1 more source

Effect of crowding on the electron transfer process from plastocyanin and cytochrome c6 to photosystem I: a comparative study from cyanobacteria to green algae [PDF]

open access: yes, 2011
Plastocyanin and cytochrome c 6, the alternate donor proteins to photosystem I, can be acidic, neutral or basic; the role of electrostatics in their interaction with photosystem I vary accordingly for cyanobacteria, algae and plants.
Hervás Morón, Manuel   +1 more
core   +1 more source

How does NO activate hemeproteins? [PDF]

open access: yesFEBS 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.
openaire   +2 more sources

Heme and iron limitation in a GI-tract foundation species leads to a reshuffling of the metalloproteome and a shift toward manganese usage

open access: yesFrontiers in Chemistry
The metal-binding complement of the cellular proteome (the metalloproteome) depends on metal availability in the cellular environment and drives cellular metabolism.
Ronivaldo Rodrigues da Silva   +3 more
doaj   +1 more source

Assessment of biochemical parameters and study its correlation in ß-Thalassemia major patients and healthy controls in Kirkuk City, Iraq

open access: yesMedical Journal of Babylon, 2020
Background: Thalassemia is the name of a group of genetically (acquired) blood diseases, which include defects on the production of hemeprotein, and fractional or complete damage to the combination of a particular sort of simple protein chain. The defect
Ismail Khalil Abd, Israa Ghassan Zainal
doaj   +1 more source

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