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Part of the book series: Progress in Inflammation Research ((PIR))

Abstract

Introduction Heme consists of a protoporphyrin ring with a tightly bound iron atom, which can exist in both a ferrous (Fe2+) and ferric (Fe3+) state, held in the centre of the molecule by four nitrogen atoms. This molecule is of fundamental importance in many biochemical pathways including oxygen transport by hemoglobin and electron transport in the respiratory chain. Heme is also a prosthetic group for numerous enzymes, which most notably in the context of this book include cyclooxygenase (COX) and nitric oxide synthesis (NOS) [1]. Heme has been demonstrated to regulate protein synthase via elf-2a kinase [2]. Therefore, maintenance of the heme pool is of considerable importance in eukaryotic systems, with the levels of intracellular heme being controlled at both the level of biosynthesis and degradation.

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Willis, D. (1999). Overview of HO-1 in inflammatory pathologies. In: Willoughby, D.A., Tomlinson, A. (eds) Inducible Enzymes in the Inflammatory Response. Progress in Inflammation Research. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8747-2_3

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  • DOI: https://doi.org/10.1007/978-3-0348-8747-2_3

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  • Print ISBN: 978-3-0348-9755-6

  • Online ISBN: 978-3-0348-8747-2

  • eBook Packages: Springer Book Archive

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