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How does NO activate hemeproteins? [PDF]
FEBS 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
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Oxidative modification of quercetin by hemeproteins
Biochemical and Biophysical Research Communications, 2006The 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.
Alexander V Baranovsky, Sergey A Usanov
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Measurement of O2 Binding by Sensory Hemeproteins
2023The 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 +1 more
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On the biosynthesis of heme and hemeproteins in liver cell
Biochimica Et Biophysica Acta, 1958Shigeki Minakami +2 more
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Rate Theories and Puzzles of Hemeprotein Kinetics
Science, 1985The binding of dioxygen and carbon monoxide to heme proteins such as myoglobin and hemoglobin has been studied with flash photolysis. At temperatures below 200 K, binding occurs from within the heme pocket and, contrary to expectation, with nearly equal rates for both ligands. This observation has led to a reexamination of the theory of the association
H, Frauenfelder, P G, Wolynes
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Theory of hemeprotein reactivity
Journal of Theoretical Biology, 1971Abstract A chemical theory of hemeprotein reactivity is presented. It is based upon recent chemical and spectroscopic studies of metalloporphyrins and hemeproteins and upon the established X-ray structures of the iron (III) complexes of hemoglobin, myoglobin and cytochrome c.
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STUDIES ON HISTIDINE RESIDUES IN HEMEPROTEINS RELATED TO THEIR ACTIVITIES
Journal of Biochemistry, 1960exaly +4 more sources
A hemeprotein implicated in oxygen transport into the eye of fish
Comparative Biochemistry and Physiology Part A: Physiology, 1975Abstract 1. 1. Following occlusion of the circulation to the eye of bluefish a ferric hemeprotein (or proteins) appears in the blood plasma of the ophthalmic blood vessels. 2. 2. This protein may play a role in the establishment of elevated oxygen pressures by the choroid rete mirabile. 3. 3.
J B, Wittenberg, B A, Wittenberg
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Permeability of the neonatal rat choriocapillaris to hemeproteins and ferritin
American Journal of Anatomy, 1982AbstractThe permeability of the endothelium of the capillaries of the rat choriocapillaris to circulating macromolecules was examined during the first postnatal week of development using hemeproteins of different molecular dimensions and ferritin. At this stage of development capillaries and photoreceptor cells in the neural retina are not fully formed,
R M, Pino, E, Essner, L C, Pino
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Syntehsis and structural stability of helichrome as an artificial hemeproteins
Biopolymers, 1990AbstractA detailed procedure is described for the syntehsis of helichrome, which is the first successful example of polypeptide‐based artificial hemeprotein. The segment synthesis‐condensation approach used for the assembly of small proteins has proven to be extremely useful for protein mimetics as well.
T, Sasaki, E T, Kaiser
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