(ORDO NEWS) — A detailed study of a recently discovered bacterial enzyme has allowed an international team of scientists to develop a new way to obtain energy directly from atmospheric air.
An extremely unusual enzyme is able to oxidize micro-concentrations of molecular hydrogen, and this can be used to create an electric current.
Thus, the study can become the basis for creating a new environmentally friendly energy source.
Oxidation of atmospheric molecular hydrogen, which takes place with the participation of various types of soil bacteria, is considered a key biogeochemical process.
They oxidize at least 75% of all hydrogen removed from the atmosphere.
This process provides bacteria with an additional source of energy in case of limited nutrient content in the soil environment, for example, in Antarctic soils, volcanic craters and deep oceans.
However, how bacteria are able to oxidize hydrogen, the content of which in the atmosphere does not exceed 0.00005 volume percent, remains a poorly studied topic.
In addition, it is not clear how bacteria manage to eliminate the effect of the catalytic poison – molecular oxygen, which should greatly reduce the efficiency of such a process.
Especially considering that the concentration of this “poison” is six orders of magnitude higher than the concentration of target hydrogen molecules.
To fill gaps in knowledge, an international team of scientists led by a team from Monash University (Australia) investigated in detail the structural and mechanistic basis of hydrogen oxidation by the bacterium Mycobacterium smegmatis.
In particular, they isolated the Huc enzyme , which is responsible for the very reaction of hydrogen oxidation and further energy generation in bacterial cells.
In addition to revealing the detailed molecular structure of the Huc protein , the authors of the study created whole films from this enzyme.
Then the films were deposited on the electrode and the generation of electricity was studied depending on the amount of hydrogen in the surrounding air.
It turned out that Huc is able to selectively bind and oxidize hydrogen up to concentrations that are limiting for measuring instruments (15 times lower than atmospheric values).
The efficiency of this binding did not depend on oxygen concentration, which means that Huc is an oxygen-insensitive enzyme. In addition, Huc proved to be an extremely stable protein.
The purified enzyme can be stored for a long period of time, frozen and heated up to 80 degrees Celsius without losing the ability to generate energy.
Despite the early stage of research, the authors are confident that the discovery of Huc, a detailed description of its structure and operation, has significant potential for creating small air-powered devices – for example, as an alternative to solar-powered devices.
Moreover, there will be no shortage of enzymes of this type: the bacteria that produce them are widespread and can be grown in large quantities.
—
Online:
Contact us: [email protected]
Our Standards, Terms of Use: Standard Terms And Conditions.