Results 191 to 200 of about 2,605 (236)
Some of the next articles are maybe not open access.
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 ...
C E, Castro +5 more
openaire +2 more sources
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
openaire +2 more sources
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.
Egor M, Cherviakovsky +6 more
openaire +2 more sources
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
semanticscholar +1 more source
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
openaire +1 more source
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.
Tapan K. Das +2 more
openaire +1 more source
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.
Tapan K. Das +2 more
openaire +1 more source
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
openaire +1 more source
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 +1 more source
Hemeproteins: Recent Advances in Quantitative XANES Analysis
AIP Conference Proceedings, 2007Recently, we have shown that multiple scattering (MS) theory, via the MXAN package, is able to reproduce the experimental X‐ray absorption near edge structure (XANES) data of biological samples, in particular hemeproteins, from the rising edge up to ∼150–200 eV above the edge.
A. ARCOVITO +3 more
openaire +1 more source
Alkaline low spin form of sulfite reductase hemeprotein subunit
Biochemical and Biophysical Research Communications, 1990The reversible reduction and reoxidation of Escherichia coli sulfite reductase hemeprotein subunit at pH 9.9 produces high and low spin ferric species, the latter with properties distinct from any alkaline low spin yet reported. With virtually no effect on the 298 degrees K optical spectrum, chloride drastically reduces the low spin EPR intensity and ...
L J, Young, L M, Siegel
openaire +2 more sources
Ultrafast absorption and Raman spectroscopy of hemeproteins
Chemical Physics, 1989Abstract The applications of Raman and absorption spectroscopy to understand the photophysics and the dynamics of hemoglobin and myoglobin are discussed. The extension of these techniques to the picosecond and the femtosecond domains is described. Study of hemeprotein reactivity on this ultrafast time scale is advantageous because it simplifies the ...
J.W. Petrich, J.L. Martin
openaire +1 more source