Results 181 to 190 of about 3,386 (219)

Directed evolution of Escherichia coli surface-displayed Vitreoscilla hemoglobin as an artificial metalloenzyme for the synthesis of 5-imino-1,2,4-thiadiazoles. [PDF]

Chem Sci
Xu Y, Li F, Xie H, Liu Y, Han W, Wu J, Cheng L, Wang C, Li Z, Wang L.   +9 more
europepmc   +1 more source

The Pharmacokinetics of Saliva and Plasma N-Oxides Following a Single Administration of a Plant-Based Bioequivalent Inorganic Nitrate Oral Supplement in an Open-Label, Phase 1, Single-Arm Study. [PDF]

J Clin Med
Stahl ME, Grammer EE, Allen JD, Weltman A.   +3 more
europepmc   +1 more source

Hemozoin: a waste product after heme detoxification? [PDF]

Parasit Vectors
Sun J, Fang C, Qin X, Si W, Wang F, Li Y, Yan X.   +6 more
europepmc   +1 more source

Wandering about allostery. [PDF]

Biol Direct
Brunori M.
europepmc   +1 more source

Hemeproteins Bathed in Ionic Liquids: Examining the Role of Water and Protons in Redox Behavior and Catalytic Function

, 2009
John J. Moran
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Tryptophan fluorescence of hemeproteins

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Hemeproteins as Targets for Sulfide Species

Antioxidants & Redox Signaling, 2020
Significance: Sulfides are endogenous and ubiquitous signaling species that share the hemeproteins as biochemical targets with O2, nitric oxide, and carbon monoxide. The description of the binding mechanisms is mandatory to anticipate the biochemical relevance of the interaction.
Boubeta, Fernando Martín, Bieza, Silvina Andrea, Bringas, Mauro, Palermo, Juan Cruz, Boechi, Leonardo, Estrin, Dario Ariel, Bari, Sara Elizabeth   +6 more
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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, E, Bartnicki, C, Robertson, R, Havlin, H, Davis, T, Osborn   +5 more
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Measurement of O2 Binding by Sensory Hemeproteins

2023
The discovery of an increasing number of proteins that function in the detoxification and sensing of gaseous ligands has renewed interest in hemeproteins. It is critical to measure the affinities of these proteins for ligands like O2, CO, and NO, know with confidence when a protein is fully saturated with a specific ligand, and be able to estimate how ...
Marie A, Gilles-Gonzalez, Eduardo H S, Sousa   +1 more
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Oxidative modification of quercetin by hemeproteins

Biochemical and Biophysical Research Communications, 2006
The ability of a number of hemeproteins to oxidize the flavonoid quercetin has been shown. It was found that quercetin undergoes chemical modification in the presence of cytochrome c, myoglobin, and hemoglobin but not cytochrome b(5). In the range of investigated proteins the most effective oxidant appears to be cytochrome c.
Egor M, Cherviakovsky, Dmitry A, Bolibrukh, Alexander V, Baranovsky, Tamara M, Vlasova, Vladimir P, Kurchenko, Andrey A, Gilep, Sergey A, Usanov   +6 more
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