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Biochim Biophys Acta. 2013 Aug-Sep;1827(8-9):938-48. doi: 10.1016/j.bbabio.2013.03.010. Epub 2013 Apr 2.

Multi-heme proteins: nature's electronic multi-purpose tool.

Author information

1
Department of Chemistry, Boston University, Boston, MA 02215, USA.

Abstract

While iron is often a limiting nutrient to Biology, when the element is found in the form of heme cofactors (iron protoporphyrin IX), living systems have excelled at modifying and tailoring the chemistry of the metal. In the context of proteins and enzymes, heme cofactors are increasingly found in stoichiometries greater than one, where a single protein macromolecule contains more than one heme unit. When paired or coupled together, these protein associated heme groups perform a wide variety of tasks, such as redox communication, long range electron transfer and storage of reducing/oxidizing equivalents. Here, we review recent advances in the field of multi-heme proteins, focusing on emergent properties of these complex redox proteins, and strategies found in Nature where such proteins appear to be modular and essential components of larger biochemical pathways. This article is part of a Special Issue entitled: Metals in Bioenergetics and Biomimetics Systems.

KEYWORDS:

Cytochrome c; Cytochrome c peroxidase; Dissimilatory metal reduction; Electron transfer

PMID:
23558243
PMCID:
PMC3880547
DOI:
10.1016/j.bbabio.2013.03.010
[Indexed for MEDLINE]
Free PMC Article

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