Journal Article
The energy‐conserving electron transfer system used by D esulfovibrio alaskensis strain G 20 during pyruvate fermentation involves reduction of endogenously formed fumarate and cytoplasmic and membrane‐bound complexes, Hdr‐Flox and Rnf
Birte Meyer; Jennifer V. Kuehl; Morgan N. Price; Jayashree Ray; Adam M. Deutschbauer; Adam P. Arkin; David A. Stahl
Environmental Microbiology · Vol. 16, Issue 11 · pp. 3463-3486 · 2014
Abstract
Summary The adaptation capability of D esulfovibrio to natural fluctuations in electron acceptor availability was evaluated by studying D esulfovibrio alaskensis strain G 20 under varying respiratory, fermentative and methanogenic coculture conditions in chemostats. Transition from lactate to pyruvate in coculture resulted in a dramatic shift in the population structure and closer interspecies cell‐to‐cell interactions. Lower methane production rates in coculture than predicted from pyruvate input was attributed to redirection of electron flow to fumarate reduction. Without a methanogenic partner, accumulation of H 2 and formate resulted in greater succinate production. Comparative transcript and gene fitness analysis in concert with physiological data of G 20 wildtype and mutants demonstrated that pyruvate fermentation involves respiration of cytoplasmically formed fumarate using cytoplasmic and membrane‐bound energy‐conserving complexes, Rnf , Hdr‐Flox ‐1 and Hmc. At the low H 2 /formate levels maintained in coculture, Rnf likely functions as proton‐pumping ferredoxin (Fd) : type‐I cytochrome c oxidoreductase, which transitions to a proton‐pumping Fd red : nicotinamide adenine dinucleotide ( NAD + ) oxidoreductase at high H 2 /formate levels during fermentation in monoculture. Hdr‐Flox ‐1 is postulated to recycle Fd red via a flavin‐based electron bifurcation involving NADH , Fd ox and the thiol/disulphide‐containing DsrC . In a menaquinone ( MQ )‐based electron confurcation reaction, the high‐molecular‐weight cytochrome‐c 3 complex, Hmc , is proposed to then couple DsrC red and periplasmic H 2 /formate oxidation using the MQ pool to fuel a membrane‐bound fumarate reductase.