Results 161 to 170 of about 1,942 (200)
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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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Helichrome: synthesis and enzymic activity of a designed hemeprotein
Journal of the American Chemical Society, 1989Tomikazu Sasaki, E. Kaiser
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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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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.
Jonathan B. Wittenberg +3 more
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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,
Richard M. Pino +2 more
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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, Jean-Louis Martin
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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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Spin and electron distributions in heme-cyanide models and hemeproteins
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985Proton NMR spectra of low-spin Fe(III) cyanoprotoheme as prosthetic group in a number of proteins are presented. The diagonally positioned 1-, 5- and 3-, 8-methyl groups obey shifts proportional to the Fe(III)/(II) reduction potential Em7, which indicates a pseudo-contact interaction.
Bo Nordén +3 more
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De Novo Designed Hemeproteins As A Redox Catalyst [PDF]
[1990] Proceedings of the Twelfth Annual International Conference of the IEEE Engineering in Medicine and Biology Society, 2005 Synthetic peptides are an attractive candidate for the assembly of biomimetic redox catalysts. We have synthesized series of hemeprotein models (helichrome) which have structured polypeptides as a building unit. Four amphiphilic ahelices were attached to the porphyrin ring covalently so that they interacted with each other to form an a-helical bundle ...
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