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Updated: Jan 7, 2026
![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
Functional insights into the nitrogenase-like enzyme superfamily
Ana Lago-Maciel1, Marcello Herzog1, Johannes G Rebelein2
1Microbial Metalloenzymes Research Group, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.
None:
Nitrogenases are the only enzymes capable of converting atmospheric nitrogen into bioavailable ammonia, an essential process for all life on Earth. Early ancestors of bona fide nitrogenases and their maturases gave rise to several structural homologues with diverse functions. The nitrogen fixation-like enzyme superfamily comprises ancient metalloproteins involved in elemental processes that range from the biosynthesis of bacteriochlorophyll in bacterial photosynthesis to the biosynthesis of cofactor F430 in archaeal methanogenesis. Recently, new functions of nitrogenase-like enzymes in sulfur scavenging were discovered and have spurred interest due to the simultaneous production of small hydrocarbons. Here we explore the structural and functional diversity of the nitrogen fixation-like enzyme superfamily and its potential for the production of chemical building blocks beyond ammonia formation.
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