Reversibility of citrate synthase allows autotrophic growth of a thermophilic bacterium

Science. 2018 Feb 2;359(6375):563-567. doi: 10.1126/science.aao2410. Epub 2018 Feb 1.

Abstract

Biological inorganic carbon fixation proceeds through a number of fundamentally different autotrophic pathways that are defined by specific key enzymatic reactions. Detection of the enzymatic genes in (meta)genomes is widely used to estimate the contribution of individual organisms or communities to primary production. Here we show that the sulfur-reducing anaerobic deltaproteobacterium Desulfurella acetivorans is capable of both acetate oxidation and autotrophic carbon fixation, with the tricarboxylic acid cycle operating either in the oxidative or reductive direction, respectively. Under autotrophic conditions, the enzyme citrate synthase cleaves citrate adenosine triphosphate independently into acetyl coenzyme A and oxaloacetate, a reaction that has been regarded as impossible under physiological conditions. Because this overlooked, energetically efficient carbon fixation pathway lacks key enzymes, it may function unnoticed in many organisms, making bioinformatical predictions difficult, if not impossible.

MeSH terms

  • Acetyl Coenzyme A / metabolism
  • Adenosine Triphosphate / metabolism
  • Autotrophic Processes*
  • Carbon Cycle*
  • Carbon Dioxide / metabolism*
  • Citrate (si)-Synthase / metabolism*
  • Citric Acid / metabolism
  • Deltaproteobacteria / enzymology*
  • Deltaproteobacteria / growth & development*
  • Oxaloacetic Acid / metabolism

Substances

  • Carbon Dioxide
  • Citric Acid
  • Oxaloacetic Acid
  • Acetyl Coenzyme A
  • Adenosine Triphosphate
  • Citrate (si)-Synthase