June 1, 2012
Journal Article

Exploring the biochemistry at the extracellular redox frontier of bacterial mineral Fe(III) respiration

Abstract

Many species of the bacterial Shewanella genus are notable for their ability to respire in anoxic environments utilizing insoluble minerals of Fe(III) and Mn(IV) as extracellular electron acceptors. In Shewanella oneidensis, the process is dependent on the decahaem electron-transport proteins that lie at the extracellular face of the outer membrane where they can contact the insoluble mineral substrates. These extracellular proteins are charged with electrons provided by an inter-membrane electron-transfer pathway that links the extracellular face of the outer membrane with the inner cytoplasmic membrane and thereby intracellular electron sources. In the present paper, we consider the common structural features of two of these outermembrane decahaem cytochromes, MtrC and MtrF, and bring this together with biochemical, spectroscopic and voltammetric data to identify common and distinct properties of these prototypical members of different clades of the outer-membrane decahaem cytochrome superfamily.

Revised: July 3, 2012 | Published: June 1, 2012

Citation

Richardson D.J., M. Edwards, G.F. White, N. Baiden, R.S. Hartshorne, J.K. Fredrickson, and L. Shi, et al. 2012. Exploring the biochemistry at the extracellular redox frontier of bacterial mineral Fe(III) respiration. Biochemical Society: Transactions 40, no. 3:493-500. PNNL-SA-88013.