Publication Cover
Redox Report
Communications in Free Radical Research
Volume 14, 2009 - Issue 3
1,387
Views
41
CrossRef citations to date
0
Altmetric
Review

Heme oxygenase and iron: from bacteria to humans

&
Pages 95-101 | Published online: 19 Jul 2013
 

Abstract

Iron and iron-containing prosthetic groups are involved in many fundamental processes that constitute life. One of the biologically most important iron-containing groups is heme, in which an iron atom is co-ordinated to a protoporphyrin ring. Heme proteins have a wide range of functions, participating in a vast repertoire of biochemical reactions. Due to its abundance, heme also serves as an important source of iron. Enzymatic degradation of heme usually involves its oxidative cleavage by heme oxygenase. Not surprisingly, heme oxygenase activity is present in organisms across different domains and kingdoms. This review summarises the current knowledge in the dynamic relationship between heme oxygenase and iron in metabolism and in the clinical context.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.