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Heme and hemoproteins

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Published by Springer-Verlag in Berlin, New York .
Written in English

Subjects:

  • Porphyria -- Etiology.,
  • Heme.,
  • Hemoproteins.,
  • Drugs -- Toxicology.,
  • Heme -- Metabolism.,
  • Liver -- Metabolism.,
  • Hemeproteins -- Metabolism.,
  • Pharmacology.,
  • Porphyria -- Chemically induced.

Book details:

Edition Notes

Includes bibliographies and indexes.

Statementcontributors, K. W. Bock ... [et al.] ; editors, Francesco De Matteis, W. Norman Aldridge.
SeriesHandbuch der experimentellen Pharmakologie :, v.44
ContributionsBock, Karl Walter., De Matteis, Francesco, 1932-, Aldridge, W. Norman.
Classifications
LC ClassificationsQP905 .H3 vol. 44, RC632.P6 .H3 vol. 44
The Physical Object
Paginationxv, 449 p. :
Number of Pages449
ID Numbers
Open LibraryOL4545388M
ISBN 100387084606
LC Control Number77013134

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Abstract. Heme cofactors are found in a wide range of proteins, where they play various roles in e.g., steroid 1 and bioactive lipid synthesis, 2 energy transduction, 3 gene regulation, 4 cellular signaling, 5 oxygen transport 6 and antibiotic biosynthesis. 7 The diversity of physiological functions performed by hemoproteins means that heme is among the most versatile of protein cofactors. 8 Cited by: ISBN: OCLC Number: Description: 1 online resource: Contents: 1 The Biosynthesis and Degradation of Heme --A. Introduction --B. Structures of Porphyrins and Hemes --C. Function and Turnover of Hemoproteins --D. Enzymes of Heme Biosynthesis and Degradation --E. Conjugation of Bilirubin --F. Control of Heme and . Request PDF | Heme and Hemoproteins | Heme cofactors are found in a wide range of proteins, where they play various roles in e.g., steroid1 and bioactive lipid synthesis,2 energy | Find, read. Topics range from methods for the analysis of tetrapyrroles,heme, and hemoproteins, to the biosynthesis and analysis of chlorophyll and bilins. Enter your mobile number or email address below and we'll send you a link to download the free Kindle App. Then you can start reading Kindle books on your smartphone, tablet, or computer - no Kindle.

C-type hemoproteins, such as cytochrome c and the bc1 complex, contain heme c, in which the two vinyl side chains of heme b are covalently attached to the protein. The great number of studies that employ porphyrin-like compounds in different chemical contexts denotes the extraordinary interdisciplinary and multidisciplinary characters of these. heme and hemoproteins handbook of experimental pharmacology softcover reprint of the original 1st ed edition by francesco de matteis editor w norman aldridge series editor isbn book description this special issue of the handbook of experimental pharmacology on heart failure. Heme proteins are among the most versatile of metalloproteins. They have one or several characteristic iron porphyrins operating as cofactors in the protein matrices (Philips, ).In nature, there are a number of different iron porphyrin variants, including, for example, heme a, heme b, heme c, and heme these heme cofactors, heme b, (also known as protoheme IX), is among the most common. A hemeprotein (or haemprotein; also hemoprotein or haemoprotein), or heme protein, is a protein that contains a heme prosthetic are very large class of heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other is bound to the protein either covalently or noncovalently or both.

Buy Heme, Chlorophyll, and Bilins: Methods and Protocols (Springer Protocols Handbooks) by Smith, Alison, Witty, Michael (ISBN: ) from Amazon's Book Store. Everyday low prices and free delivery on eligible : Hardcover. MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price. Bacteria that are able to bind or utilize heme or hemoproteins but have uncharacterized heme assimilation systems. Citation: Perkins-Balding D, Rasmussen A, Stojiljkovic I. Bacterial Heme and Hemoprotein Receptors, p Keywords:Heme biosynthesis, Heme metabolism, Heme related disorders, CYP, Genetic defects, Drug metabolism. Abstract:Heme is central to functions of many biologically important enzymes (hemoproteins). It is an assembly of four porphyrin rings joined through methylene bridges with a . This chapter describes hemophore secretion and its interaction with heme and hemoproteins, specific receptors, mechanisms of heme transfer from hemophore to receptor, TonB function at various steps in the heme acquisition process, and the regulation of the has operon. HasA hemophores are secreted by ABC transporters.