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


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.

SUBMITTER: Bewley KD 

PROVIDER: S-EPMC3880547 | biostudies-literature | 2013 Aug-Sep

REPOSITORIES: biostudies-literature

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

Bewley Kathryn D KD   Ellis Katie E KE   Firer-Sherwood Mackenzie A MA   Elliott Sean J SJ  

Biochimica et biophysica acta 20130402 8-9


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  ...[more]

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