Results 151 to 160 of about 2,121 (177)

Ultrafast absorption and Raman spectroscopy of hemeproteins

Chemical Physics, 1989
Abstract 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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Spin and electron distributions in heme-cyanide models and hemeproteins

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
Proton 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.
J, Paul, M L, Smith, B, Nordén, K G, Paul   +3 more
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Do the hemeproteins behave as a dissipative structure?

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 ...
Bernard Alpert, V�ronique Le Tilly, Serge Pin, Olivier Sire, Christian Zentz   +4 more
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Optical rotatory dispersion of a respiratory hemeprotein of Chrinomus thummi

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1968
Abstract The spatial structure of an O 2 -binding hemeprotein obtained from Chironomus thummi is compared with that of sperm whale myoglobin by means of rotatory dispersion. The optical rotation at the 233-mμ minimum of the ultraviolet Cotton effect is only 70% of the value obtained for myoglobin.
H, Formanek, J, Engel
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Azanone (HNO) interaction with Hemeproteins and metalloporphyrins

2012
Abstract Azanone (HNO), also called nitroxyl, is a highly reactive compound, with interesting yet poorly understood biological properties. Like its closely related sibling NO, its main biological targets are heme proteins, although significant differences in their reactivity and pharmacological effects are observed.
Doctorovich, Fabio, Bikiel, Damian Ezequiel, Pellegrino, Juan, Suarez, Sebastian, Marti, Marcelo Adrian   +4 more
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PI‐INTERACTIONS IN METALLOPORPHYRINS AND HEMEPROTEINS*

Annals of the New York Academy of Sciences, 1969
W S, Caughey, H, Eberspaecher, W H, Fuchsman, S, McCoy, J O, Alben   +4 more
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Protein Fluctuations and Hemeprotein Affinity for Ligand

1986
Binding 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.
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Vibrational Circular Dichroism of Ligand Vibrations in Hemeprotein

1995
The distal amino acid residues in myoglobin (Mb) and hemoglobin (Hb) are elaborately designed to control the chemical reactions of ligands to the heme iron. Many techniques have been applied to elucidate the reaction mechanism of ligand binding in heme pockets.
J. Teraoka, N. Yamamoto, Y. Matsumoto, Y. Kyogoku, H. Sugeta   +4 more
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Heme oxygenase-1 protects against inflammatory and apoptosis induced by hemeproteins in Ctenopharyngodon Idellus kidney cells

Aquaculture, 2022
Zhijie Lu, Fanbin Zhan, Li Lin
exaly  

CARBON MONOXIDE BONDING IN HEMEPROTEINS *

Annals of the New York Academy of Sciences, 1970
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