Third form of life makes energy in 'remarkable' ways, scientists discover
An international team of researchers discovered at least nine phyla of archaea, a domain of single-celled organisms lacking internal membrane-bound structures, that produce hydrogen gas using 'ultraminimal' enzymes thought to only exist in the other two forms of life
In a shake up of the biological order, scientists have discovered that the third form of life, archaea, has been using hydrogen instead of oxygen to generate energy, says ScienceAlert.
An international team of researchers discovered at least nine phyla of archaea, a domain of single-celled organisms lacking internal membrane-bound structures, that produce hydrogen gas using 'ultraminimal' enzymes thought to only exist in the other two forms of life.
Archaea, they realised, not only have the smallest hydrogen-using enzymes compared to bacteria and eukaryotes, but their enzymes for consuming and producing hydrogen are also the most complex characterised so far.
Small and mighty, these enzymes have seemingly allowed archaea to survive and thrive in some of Earth's most hostile environments where little to no oxygen is found.
"Humans have only recently begun to think about using hydrogen as a source of energy, but archaea have been doing it for a billion years," says Pok Man Leung, a microbiologist at Monash University in Australia who co-led the study.
"Biotechnologists now have the opportunity to take inspiration from these archaea to produce hydrogen industrially."
Hydrogen is the most abundant element in the Universe and is used globally to make fertilisers and other chemicals, treat metals, process foods, and refine fuels.
But hydrogen's future lies in energy storage and steel-making, which could be produced with zero emissions if renewable energy is used to convert materials such as water into hydrogen gas.
Microorganisms produce and release hydrogen gas (H2) for entirely different purposes, mainly to dispose of excess electrons produced during fermentation, a process whereby organisms extract energy from carbohydrates such as sugars without oxygen.
Enzymes used for consuming or producing H2 are called hydrogenases, and they were first comprehensively surveyed across the tree of life only eight years ago. Since then, the number of known microbial species has exploded, particularly archaea, which hide out in extreme environments, such as hot springs, volcanoes, and deep-sea vents.
However, most archaea are known only from chunks of their genetic code found in these environments, and many haven't been cultured in the lab because it's very difficult to do so.
So Monash University microbiologist Chris Greening and colleagues searched for the gene encoding part of one type of hydrogenase, fast-acting [FeFe] hydrogenases, in more than 2,300 archaeal species clusters listed in a global database.
Then they tasked Google's AlphaFold2 with predicting the structure of the encoded enzymes, and expressed those enzymes in E. coli bacteria, to check those genes were actually functional and produced hydrogenases capable of catalysing hydrogen reactions in their surrogate host.
"Our finding brings us a step closer to understanding how this crucial process gave rise to all eukaryotes, including humans," Leung says.
Eukaryotes are organisms whose cells contain a nucleus and membrane-bound organelles, such as mitochondria and other useful cellular factories.
All eukaryotes are thought to have emerged from the union of an anaerobic archaea and a bacterium it gobbled up billions of years ago. A second, much later endosymbiosis then gave rise to the ancestor of plants, with chloroplasts.
Greening, Leung, and their colleagues found the genetic instructions for [FeFe] hydrogenases in nine archaeal phyla and confirmed they are indeed active in those microorganisms – making it three from three domains of life that use these kinds of enzymes to make hydrogen.
But unlike bacteria and eukaryotes, further analyses showed that archaea assemble "remarkable hybrid complexes" for their hydrogen production needs, fusing two types of hydrogenases together.
"These findings reveal new metabolic adaptations of archaea, streamlined H2 catalysts for biotechnological development, and a surprisingly intertwined evolutionary history between the two major H2-metabolising enzymes," the team writes in their paper.
Many of the catalogued archaea genomes analysed in this study are, however, incomplete, and who knows how many more species are yet to be discovered
It's more than likely that archaea harbour other ingenious ways of making energy that we are yet to find.
The research has been published in Cell.