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Biological Chemistry, 2022
Abstract Heme (protoheme IX) is an essential cofactor for a large variety of proteins whose functions vary from one electron reactions to binding gases. While not ubiquitous, heme is found in the great majority of known life forms. Unlike most cofactors that are acquired from dietary sources, the vast majority of organisms that utilize ...
Harry A. Dailey, Amy E. Medlock
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Abstract Heme (protoheme IX) is an essential cofactor for a large variety of proteins whose functions vary from one electron reactions to binding gases. While not ubiquitous, heme is found in the great majority of known life forms. Unlike most cofactors that are acquired from dietary sources, the vast majority of organisms that utilize ...
Harry A. Dailey, Amy E. Medlock
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Defects in the biosynthesis of mitochondrial heme c and heme a in yeast and mammals
Biochimica Et Biophysica Acta - Bioenergetics, 2004 Defects in heme biosynthesis have been associated with a large number of diseases, but mostly recognized in porphyrias, which are neurovisceral or cutaneous disorders caused by the accumulation of biosynthetic intermediates.
CARLOS T Moraes, Antoni Barrientos
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Heme biosynthesis in the heart
Biochemical Pharmacology, 1982The rates of biosynthesis of heme a and heme b in hearts of fed and fasted rats were measured using an isolated heart perfusion system. delta-Aminolevulinic acid synthetase activity was decreased in hearts of fasted rats to about 30% of values in hearts obtained from fed rats.
R, Sedman +3 more
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The biochemistry of heme biosynthesis
Archives of Biochemistry and Biophysics, 2008Heme is an integral part of proteins involved in multiple electron transport chains for energy recovery found in almost all forms of life. Moreover, heme is a cofactor of enzymes including catalases, peroxidases, cytochromes of the P(450) class and part of sensor molecules.
Ilka U, Heinemann +2 more
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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 ...
M Scott, Morrison +2 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.
openaire +2 more sources