One enzyme is enough to convert air into energy. An amazing achievement for scientists

The authors of the post published in Pages are behind this hack naturewho performed species-specific analyses Mycobacterium smear. These bacteria can survive even in environments that seem completely unsuitable for life. However, these nutrient-poor places are not an insurmountable obstacle for them M. smegmatis.

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And according to the research that was done, it’s all thanks to an enzyme that the members of the research team named hook. It is he who makes it possible to obtain energy from the hydrogen in the air, which should be especially useful to people. Of course, the benefit would be minimal if researchers failed to identify the main mechanism that leads to such a desirable effect.

The authors were able to isolate and then analyze the enzyme in question in detail. They argue that a similar mechanism could be used to power a range of small portable electrical devices. Specific examples include biometric sensors, environmental monitors, digital clocks and calculators, or simple computers.

M. smegmatis generates electricity from hydrogen thanks to an enzyme called Huc

The research team was led by Reese Grinter of Monash University. The scientist asserts that the more hydrogen the enzyme has at its disposal, the more electricity it can produce. That’s why, with hydrogen concentrated properly, it should be possible to power more advanced devices, such as smartwatches, smartphones, laptops, and maybe even cars.

Interestingly, M. smegmatis Because of its relationship to bacteria Mycobacterium tuberculosisResponsible for tuberculosis – often used in laboratory research. Because of this, her extraordinary abilities were known to the science world in the past. This intriguing bacterium has so far been found in Antarctica, volcanic craters, and the deep oceans, among other places.

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In their search for the Huc enzyme, the scientists used chromatography to separate the components of the mixture. They later studied the enzyme’s atomic structure using cryo-electron microscopy. Thanks to this, it was possible to determine that the described bacteria have a structure containing charged ions of nickel and iron. When hydrogen molecules (consisting of two protons and two electrons) enter this region, they become trapped between the nickel and iron ions and are stripped of their electrons. The enzyme then sends out these electrons to generate electricity.

It is very important to store the isolated enzyme for a long time and it can withstand temperatures below zero and up to 80°C. In addition, hydrogen at a concentration of only 0.00005% of what is present in the air we breathe is sufficient to generate electricity. It appears to be a very efficient source of energy that humanity can draw from.