Beyond the genome: functional studies of phototrophic sulfur oxidation.
The increasing availability of complete genomic sequences for cultured phototrophic bacteria and assembled metagenomes from environments dominated by phototrophs has reinforced the need for a "post-genomic" analytical effort to test models of cellular structure and function proposed from genomic data. Comparative genomics has produced a testable model for pathways of sulfur compound oxidation in the phototrophic bacteria. In the case of sulfide, two enzymes are predicted to oxidize sulfide: sulfide:quinone oxidoreductase and flavocytochrome c sulfide dehydrogenase. However, these models do not predict which enzyme is important under what conditions. In Chlorobaculum tepidum, a model green sulfur bacterium, a combination of genetics and physiological analysis of mutant strains has led to the realization that this organism contains at least two active sulfide:quinone oxidoreductases and that there is significant interaction between sulfide oxidation and light harvesting. In the case of elemental sulfur, an organothiol intermediate of unknown structure has been proposed to activate elemental sulfur for transport into the cytoplasm where it can be oxidized or assimilated, and recent approaches using classical metabolite analysis have begun to shed light on this issue both in C. tepidum and the purple sulfur bacterium Allochromatium vinosum.
College of Earth, Ocean and Environment and Delaware Biotechnology Institute and Department of Biological Sciences, University of Delaware, Newark, DE 19711, USA. tehanson@udel.edu
Thomas E
TE
Hanson
Rachael M
RM
Morgan-Kiss
Leong-Keat
LK
Chan
Jennifer
J
Hiras
D019414:Chlorobi / Q000235:genetics / Q000378:metabolism*; D002841:Chromatiaceae / Q000235:genetics / Q000378:metabolism*; D016680:Genome, Bacterial; D010084:Oxidation-Reduction; D011808:Quinone Reductases / Q000378:metabolism*; D013440:Sulfides / Q000737:chemistry*; D013455:Sulfur / Q000737:chemistry*
D013440:Sulfides; D013455:Sulfur; D011808:Quinone Reductases