Results 321 to 330 of about 339,218 (339)
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Multiheme proteins: effect of heme–heme interactions
Dalton Transactions, 2018This Frontier illustrates a brief personal account on the effect of heme–heme interactions in dihemes which thereby discloses some of the evolutionary design principles involved in multiheme proteins for their diverse structures and functions.
Dipti Lai +2 more
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Environmental Heme Utilization by Heme-Auxotrophic Bacteria
2012Heme, an iron-containing porphyrin, is the prosthetic group for numerous key cellular enzymatic and regulatory processes. Many bacteria encode the biosynthetic enzymes needed for autonomous heme production. Remarkably, however, numerous other bacteria lack a complete heme biosynthesis pathway, yet encode heme-requiring functions.
Gruss, Alexandra +2 more
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Transfer of heme from heme-albumin to hemopexin
Biochimica et Biophysica Acta (BBA) - General Subjects, 1976Exchange of heme in vitro between two heme-binding serum proteins, albumin and hemopexin, was examined spectrophotometrically. Hemopexin, albumin and heme in molar ratios of 1 : 70 : 1 were incubated at 22 degrees C, pH 7.3. The heme was added as free heme, heme-hemopexin or methemalbumin. Due to the high affinity of hemopexin for heme, Kd near 10(-13)
U Muller-Ebergard +3 more
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EcoSal Plus, 2007
This review is concerned specifically with the structures and biosynthesis of hemes in E. coli and serovar Typhimurium. However, inasmuch as all tetrapyrroles share a common biosynthetic pathway, much of the material covered here is applicable to tetrapyrrole biosynthesis in other organisms.
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This review is concerned specifically with the structures and biosynthesis of hemes in E. coli and serovar Typhimurium. However, inasmuch as all tetrapyrroles share a common biosynthetic pathway, much of the material covered here is applicable to tetrapyrrole biosynthesis in other organisms.
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Biochemical and Biophysical Research Communications, 1970
Abstract EPR studies at low temperature on the ferriheme undecapeptide of cytochrome c at alkaline pH in the aggregate state reveal a quite broadened low-spin heme absorption. Successive cycles of reduction and reoxidation cause a slight change in the aggregate. The g-values of this aggregate are at 3.03, 2.16 and 1.46.
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Abstract EPR studies at low temperature on the ferriheme undecapeptide of cytochrome c at alkaline pH in the aggregate state reveal a quite broadened low-spin heme absorption. Successive cycles of reduction and reoxidation cause a slight change in the aggregate. The g-values of this aggregate are at 3.03, 2.16 and 1.46.
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Processing of Heme and Heme-Containing Proteins by Bacteria
DNA and Cell Biology, 2002An extensive amount of new knowledge on bacterial systems involved in heme processing has been accumulated in the last 10 years. We discuss common themes in heme transport across bacterial outer and inner membranes, emphasizing proteins and mechanisms involved.
Donna Perkins-Balding, Igor Stojiljkovic
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The source of heme for vascular heme oxygenase I: heme uptake in rat aorta
Canadian Journal of Physiology and Pharmacology, 2004During the last decade, heme oxygenase (HO) and carbon monoxide (CO) have garnered substantial research interest in terms of cell and organ regulation, especially as they bear on the central nervous system, organ transplantation, and the cardiovascular system. While the enzymatic mechanism, substrates, and products of HO are well known, it is not clear
Gerald S. Marks +8 more
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Kinetics of heme interaction with heme-binding proteins: The effect of heme aggregation state
Biochimica et Biophysica Acta (BBA) - General Subjects, 1997The kinetics of the interaction of heme with hemopexin and albumin was monitored by measuring the time dependence of changes in the Soret absorption spectra. Since the protein binding sites can only bind heme monomers, the binding kinetics apparently reflected the slow dissociation of heme dimers, resulting from dimer/monomer equilibria in aqueous heme
Zbyněk Hrkal +2 more
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The Janus Nature of Heme [PDF]
ChemInform, 2007 AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
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2017
Heme biosynthesis requires several metabolic steps that start with the synthesis of δ-aminolevulinic acid by δ-aminolevulinate synthase. Then, porphobilinogen is formed by δ-aminolevulinate dehydrase. Uroporphyrinogen I synthase joins four molecules of porphobilinogen to form uroporphyrinogen, a tetrapyrrole ring. After oxidations and decarboxylations,
Antonio Blanco, Gustavo Blanco
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Heme biosynthesis requires several metabolic steps that start with the synthesis of δ-aminolevulinic acid by δ-aminolevulinate synthase. Then, porphobilinogen is formed by δ-aminolevulinate dehydrase. Uroporphyrinogen I synthase joins four molecules of porphobilinogen to form uroporphyrinogen, a tetrapyrrole ring. After oxidations and decarboxylations,
Antonio Blanco, Gustavo Blanco
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