Energy conservation via electron bifurcating ferredoxin reduction and proton/Na+ translocating ferredoxin oxidation

TL;DR: In this paper , the authors focus on the nature and biosynthetic pathways of some organic redox cofactors that participate in the photosynthetic systems: quinones, chlorophyll and heme rings and their attached isoprenoid side chains, as well as on the coupled proton motive forces and associated carbon fixation pathways.

TL;DR: In this article , a 2.3 Å electron cryo-microscopy structure of HydABC is presented, which shows a heterodecamer composed of two independent 'halves' each made of two strongly interacting HydABC heterotrimers electrically connected via a [4Fe-4S] cluster.

TL;DR: In this article, the authors proposed that isoprenoids enhance the stability of fatty acid membranes at the emergence of life potentially leading to an early lipid divide and proposed a method to detect early lipid divides.

TL;DR: In this article , Tungsten-dependent aldehyde oxidoreductases (AOR) catalyse the oxidation of aldehydes to acids and are the only known enzymes reducing non-activated acids using electron donors with low redox potentials.

TL;DR: In methanogens with cytochromes, the first and last steps in methanogenesis from CO2 are coupled chemiosmotically, whereas in methenogens without cyto Chromes, these steps are energetically coupled by a cytoplasmic enzyme complex that mediates flavin-based electron bifurcation.

TL;DR: The data and analyses presented here highlight the ability to identify organizing metabolic principles from systems-level absolute metabolite concentration data, and facilitate efficient flux reversibility given thermodynamic and osmotic constraints.

TL;DR: A three-dimensional structure for the monomeric iron-containing hydrogenase (CpI) from Clostridium pasteurianum was determined, providing insights into the mechanism of biological hydrogen activation and has broader implications for [Fe-S] cluster structure and function in biological systems.

TL;DR: An overview of the nitrogenase system is presented in this article that emphasizes the structural organization of the proteins and associated metalloclusters that have the remarkable ability to catalyse nitrogen fixation under ambient conditions.