Results 181 to 190 of about 2,618 (230)
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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.
C. E. Castro
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Hemeproteins as Targets for Sulfide Species
Antioxidants & Redox Signaling, 2020Significance: 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.
Silvina A. Bieza +8 more
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The remarkable P450s: a historical overview of these versatile hemeprotein catalysts
The FASEB Journal, 1996R. Estabrook
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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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Protein Fluctuations and Hemeprotein Affinity for Ligand
, 1986Binding processes in hemeproteins involve the iron atom and the protein properties: structural and dynamics. Crystallographic data of Perutz have given an appreciate popularity to a correlation between the displacement of the iron out of the porphyrin plane and the affinity of the hemeprotein for ligand.
B. Alpert
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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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Engineering Living Biosensors using the Hemeprotein Transcription Factor CooA
The FASEB Journal, 2019Biosensors are devices that detect the presence of a biological compound. Currently biosensors have applications in food safety, medical diagnosis, and environmental monitoring.
Austin Kevon Murchison, R. Esquerra
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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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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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