Results 311 to 320 of about 339,218 (339)
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Heme-heme interaction in cytochrome oxidase
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1972Abstract The cytochromes a and a 3 of intact pigeon heart mitochondria are shown to contribute equally to the α band of cytochrome oxidase in the absence of added ligands. The oxidation-reduction midpoint potentials of the cytochromes a and a 3 at pH 7·2 are −220 mV and +380 mV, respectively.
E.S. Brocklehurst +2 more
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Evidence of heme-heme interaction in heme-spin-labeled hemoglobin
Biochemical and Biophysical Research Communications, 1971Summary Two kinds of valency hybrid hemoglobins containing spin-labeled ferric heme in one type of subunit were prepared. The electron paramagnetic resonance spectra of the α-(αSLFe +++ -βFe ++ O 2 ) and 3-(α-Fe ++ O 2 -βSLFe +++ ) spin-labeled hemoglobins were different, suggesting their non-equivalent conformational properties in hemoglobin ...
Toshio Asakura, H.R. Drott
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Chemistry – A European Journal, 2007
AbstractThe ions formally corresponding to protonated heme [FeII–hemeH]+ have been obtained by collision‐induced dissociation from the electrospray ionization of microperoxidase (MP11) and their gas‐phase chemistry has been studied by FTICR mass spectrometry.
CHIAVARINO, Barbara +3 more
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AbstractThe ions formally corresponding to protonated heme [FeII–hemeH]+ have been obtained by collision‐induced dissociation from the electrospray ionization of microperoxidase (MP11) and their gas‐phase chemistry has been studied by FTICR mass spectrometry.
CHIAVARINO, Barbara +3 more
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The role of the heme propionates in heme biochemistry
Journal of Inorganic Biochemistry, 2006There are numerous studies, relying on both experimental and theoretical observations, illustrating the active role of the heme propionates in regulating electron delivery to the iron center as well as biochemical properties of the heme. Evidences for this come from a wide variety of heme containing systems: cytochromes, heme peroxidases, globins, etc.
Brett N. Olsen, Victor Guallar
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Mechanism of heme degradation by heme oxygenase
Journal of Inorganic Biochemistry, 2000Heme oxygenase catalyzes the three step-wise oxidation of hemin to alpha-biliverdin, via alpha-meso-hydroxyhemin, verdoheme, and ferric iron-biliverdin complex. This enzyme is a simple protein which does not have any prosthetic groups. However, heme and its two metabolites, alpha-meso-hydroxyhemin and verdoheme, combine with the enzyme and activate ...
Catharina T. Migita, Tadashi Yoshida
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Is the host heme incorporated in microbial heme‐proteins?
IUBMB Life, 2008[No abstract available]
Federica Tiburzi +2 more
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Different Faces of the Heme-Heme Oxygenase System in Inflammation [PDF]
Pharmacological Reviews, 2003 The heme-heme oxygenase system has recently been recognized to possess important regulatory properties. It is tightly involved in both physiological as well as pathophysiological processes, such as cytoprotection, apoptosis, and inflammation. Heme functions as a double-edged sword.
Wagener, F.A.D.T.G. +6 more
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Die Naturwissenschaften, 1970
Some of the general concepts which have emerged in the elucidation of the biochemical reactions and transformations which occur in living organisms, summarized very briefly, are that the basic chemical reactions in the cell are rather simple, that the celt synthesizes its complex molecules from relatively simple and available substances and that there ...
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Some of the general concepts which have emerged in the elucidation of the biochemical reactions and transformations which occur in living organisms, summarized very briefly, are that the basic chemical reactions in the cell are rather simple, that the celt synthesizes its complex molecules from relatively simple and available substances and that there ...
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The concentration dependence of the heme heme interaction of hemoglobin S
Biochemical Medicine, 1976Abstract Data for oxygen equilibrium curves for Hb SS erythrocytes, both before and after separation into fractions of varying density by ultracentrifugation technique, were fitted to Hill plots and the ‘n’ values, which is a measure of the heme heme interaction of the Hb molecule, were analyzed.
Michael Seakins, Muthuraman Jayalakshmi
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The Biosynthesis of Heme O and Heme A Is Not Regulated by Copper
Biochemistry, 2005Heme A is an obligatory cofactor in all eukaryotic and many prokaryotic cytochrome c oxidase (CcO) enzymes. Despite its obvious importance to CcO and the electron transport pathway, essentially nothing is known concerning the regulation of heme A. Because CcO is the only natural target for heme A and copper is also required for CcO activity, it was ...
Eric L. Hegg +2 more
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