Hydrogen gas is a green energy carrier. Microorganisms use dedicated enzymes called hydrogenases to convert this gas into energy. One of the model enzymes is [Fe]-hydrogenase (Hmd) that catalyzes the reversible hydride transfer between H2 and the methanogenic C1-carrier tetrahydromethanopterin using a unique prosthetic group, the FeGP cofactor. Up to now, Hmd, its paralogue (HmdII), and the FeGP cofactor were identified only in archaea. Scientists at the Max Planck Institute for Terrestrial Microbiology in Marburg and collaborators at the Max Plank Institute for Biophysics in Frankfurt and Freie Universität Berlin now discovered that bacteria are also able to produce HmdII and the FeGP cofactor, and showed that bacterial HmdII uses the bacterial C1-carrier, tetrahydrofolate. This finding has a great potential for biotechnological development of Hmd variants that function in bacteria.