From low- to high-potential bioenergetic chains: Thermodynamic constraints of Q-cycle function.

The electrochemical parameters of all cofactors in the supercomplex formed by the Rieske/cytb complex and the SoxM/A-type O2-reductase from the menaquinone-containing Firmicute Geobacillus stearothermophilus were determined by spectroelectrochemistry and EPR redox titrations. All redox midpoint potentials (Em) were found to be lower than those of ubi- or plastoquinone-containing systems by a value comparable to the redox potential difference between the respective quinones. In particular, Em values of +200mV, -360mV, -220mV and -50mV (at pH7) were obtained for the Rieske cluster, heme bL, heme bH and heme ci, respectively.

Living on acetylene. A primordial energy source.

The tungsten iron-sulfur enzyme acetylene hydratase catalyzes the conversion of acetylene to acetaldehyde by addition of one water molecule to the C-C triple bond. For a member of the dimethylsulfoxide (DMSO) reductase family this is a rather unique reaction, since it does not involve a net electron transfer. The acetylene hydratase from the strictly anaerobic bacterium Pelobacter acetylenicus is so far the only known and characterized acetylene hydratase.

On the universal core of bioenergetics.

Living cells are able to harvest energy by coupling exergonic electron transfer between reducing and oxidising substrates to the generation of chemiosmotic potential. Whereas a wide variety of redox substrates is exploited by prokaryotes resulting in very diverse layouts of electron transfer chains, the ensemble of molecular architectures of enzymes and redox cofactors employed to construct these systems is stunningly small and uniform. An overview of prominent types of electron transfer chains and of their characteristic electrochemical parameters is presented.