Multiple Rieske proteins in prokaryotes: where and why?

Biochim Biophys Acta. 2005 Nov 15;1710(1):1-12. doi: 10.1016/j.bbabio.2005.09.003. Epub 2005 Oct 6.

Abstract

Many microbial genomes have been sequenced in the recent years. Multiple genes encoding Rieske iron-sulfur proteins, which are subunits of cytochrome bc-type complexes or oxygenases, have been detected in many pro- and eukaryotic genomes. The diversity of substrates, co-substrates and reactions offers obvious explanations for the diversity of the low potential Rieske proteins associated with oxygenases, but the physiological significance of the multiple genes encoding high potential Rieske proteins associated with the cytochrome bc-type complexes remains elusive. For some organisms, investigations into the function of the later group of genes have been initiated. Here, we summarize recent finding on the characteristics and physiological functions of multiple high potential Rieske proteins in prokaryotes. We suggest that the existence of multiple high potential Rieske proteins in prokaryotes could be one way of allowing an organism to adapt their electron transfer chains to changing environmental conditions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Archaeal Proteins / chemistry
  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Electron Transport Complex III / chemistry
  • Electron Transport Complex III / genetics
  • Electron Transport Complex III / metabolism*
  • Iron-Sulfur Proteins / chemistry
  • Iron-Sulfur Proteins / genetics
  • Iron-Sulfur Proteins / metabolism*
  • Phylogeny
  • Prokaryotic Cells / chemistry
  • Prokaryotic Cells / metabolism*

Substances

  • Archaeal Proteins
  • Bacterial Proteins
  • Iron-Sulfur Proteins
  • Rieske iron-sulfur protein
  • Electron Transport Complex III