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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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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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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
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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.
Tapan K. Das +2 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
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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
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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
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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
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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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Low temperature optical spectroscopy of low-spin ferric hemeproteins
European Biophysics Journal, 1996We report the Soret absorption spectra (500-350 nm) of the cyanomet derivatives of human hemoglobin and horse myoglobin, in the temperature range 300-20 K and in two different solvents (65% v/v glycerol-water or 65% v/v ethylene glycol-water). In order to obtain information on stereodynamic properties of active site of the two hemeproteins, we perform ...
M, Leone, A, Cupane, L, Cordone
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