Authors
Starwalt-Lee, R., Gralnick, J. A., Bond, D. R.
Abstract
Multiheme cytochromes are the central catalysts of extracellular electron transfer and are uniquely abundant in the genomes of model Fe(III)-reducing organisms like Geobacter sulfurreducens. While specific functions for some multiheme cytochromes are known, the complex repertoire present in any genome makes annotation and prediction of electron transfer circuitry challenging. Here we examine patterns of conservation and rates of evolutionary change among multiheme cytochromes that help explain these difficulties. Using the Ppc and OmcS cytochromes as examples we show that sequence based methods of determining protein homology can be inadequate for distinguishing between cytochromes known to have differing functions. Importantly, using mutation rate analysis, we find that multiheme cytochromes in Geobacter and Shewanella exhibit increased mutation rates, which may account for inaccurate homolog identification even between closely related organisms. Finally, an analysis of multiheme cytochrome diversity reveals that each Geobacter genome contains a high proportion of cytochromes that are unique to that individual species, suggesting a high rate of horizontal acquisition and gene loss. These increased mutational and genetic exchange rates will need to be properly accounted for in annotation tools before we can accurately ascribe function and catalog the complex repertoire of cytochromes essential to extracellular electron transfer.
Preprint server:
bioRxiv
The authors list and abstract were imported from bioRxiv on 07 Nov 2025.
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