Results 141 to 150 of about 2,013 (172)
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OXIDATION‐REDUCTION REACTIONS OF HEMEPROTEINS
Annals of the New York Academy of Sciences, 1975iiiii 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 ...
Colin Robertson +5 more
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Vibrational Energy Flow in Hemeproteins
19th International Conference on Ultrafast Phenomena, 2014We 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
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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.
Andrey Gilep +6 more
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In Silico Insight into the Reductive Nitrosylation of Ferric Hemeproteins
Inorganic Chemistry, 2020A 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
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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
Hans Frauenfelder, Peter G. Wolynes
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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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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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Proceedings / Indian Academy of Sciences, 1995
Structural change due to acid-alkaline transition in hemeproteins were monitored by circular dichroism measurements in the Soret region. It was observed that in cytochrome c and horseradish peroxidase, alkaline transition results in a large change in the heme CD due to significant conformational change in the heme cavity region.
Samaresh Mitra +2 more
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Structural change due to acid-alkaline transition in hemeproteins were monitored by circular dichroism measurements in the Soret region. It was observed that in cytochrome c and horseradish peroxidase, alkaline transition results in a large change in the heme CD due to significant conformational change in the heme cavity region.
Samaresh Mitra +2 more
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Do the hemeproteins behave as a dissipative structure? [PDF]
International Journal of Quantum Chemistry, 1996 Continuing the search for a broader interpretation of hemeprotein behavior, we give preliminary results showing that there are electric and dynamic couplings between the heme group and amino acid residues within the protein matrix. EPR and X-ray absorption spectroscopy studies on azidometmyoglobin show that both magnetic and geometric properties of ...
Olivier Sire +4 more
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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
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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