In the deep-sea environment of the East Pacific Rise, where sunlight does not penetrate and the surroundings are known for their extreme temperatures, skull-crushing pressures, and toxic compounds, lives Riftia […]
Aminotransferases (ATs) are an ancient enzyme family that play central roles in core nitrogen metabolism essential to all organisms. However, many of the AT enzyme functions remain poorly defined, limiting […]
Life is an exergonic chemical reaction. Many individual reactions in metabolism entail slightly endergonic processes that are coupled to free energy release, typically as ATP hydrolysis, in order to go […]
A new report uncovers how hydrogen gas, the energy of the future, provided energy in the past, at the origin of life 4 billion years ago.
The evolution of oxygenic photosynthesis during the Archean (4-2.5 Ga), required the presence of complementary reducing pathways to maintain the cellular redox balance.
Few described archaeal, and fewer bacterial, lineages thrive at salt-saturating conditions, such as solar saltern crystallizers (salinity above 30%-w/v).
Secrets of photosynthesis have been discovered at atomic level, shedding important new light on this plant super-power that greened the earth more than a billion years ago.
Roughly 4 billion years ago, Earth was developing conditions suitable for life. Origin-of-life scientists often wonder if the type of chemistry found on the early Earth was similar to what […]
Single-celled organisms, such as bacteria and archaea, have developed many ways to communicate with each other. For example, they might use tiny so-called extracellular vesicles (EVs) – membrane-enveloped packages smaller […]
![NifH2 cycle of Mo-nitrogenase. The NifH2 homodimer is shown in blue; it houses two nucleotide binding sites and a [4Fe-4S] redox active cluster. One catalytic half (NifDK) of the NifD2K2 heterotetramer is shown in yellow (K) and green (D); each catalytic half houses one [8Fe-7S] (Pcluster) and a [7Fe-9S-Mo-C-homocitrate] (FeMo-co) active site metallocluster. When NifH2 binds to NifDK an electron is transferred from the [4Fe-4S] cluster to FeMo-co mediated by P-cluster. NifH2 then hydrolyzes 2 ATP, dissociates with MgADP bound and an oxidized [4Fe4S] cluster. MgADP is then exchanged for MgATP and the [4Fe-4S] cluster is reduced, preparing NifH2 for binding and electron transfer. -- biorxiv.org](https://i0.wp.com/astrobiology.com/wp-content/uploads/2024/02/The-Origins-of-ATP.png?resize=1200%2C717&ssl=1)
Life depends on a conserved set of chemical energy currencies that are relics of early biochemistry. One of these is ATP, a molecule that, when paired with a divalent metal […]
