Bioassembly of complex iron–sulfur enzymes: hydrogenases and nitrogenases

• Published in: Nature reviews. Chemistry Vol. 4; no. 10; pp. 542 - 549
• Main Authors: Britt, R. David, Rao, Guodong, Tao, Lizhi
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.10.2020; Nature Publishing Group
• Subjects: 639/638; 639/638/60; Analytical Chemistry; Biochemistry; Biosynthesis; Catalysis; Chemical synthesis; Chemistry; Chemistry and Materials Science; Chemistry/Food Science; Enzymes; Hydrogenase; In vitro methods and tests; Inorganic Chemistry; Intermetallic compounds; Iron; Iron compounds; Metal clusters; Nickel compounds; Organic Chemistry; Perspective; Physical Chemistry; Redox reactions; Sulfur
• ISSN: 2397-3358; 2397-3358
• DOI: 10.1038/s41570-020-0208-x

Nature uses multinuclear metal clusters to catalyse a number of important multielectron redox reactions. Examples that employ complex Fe–S clusters in catalysis include the Fe–Mo cofactor (FeMoco) of nitrogenase and its V and all-Fe variants, and the [FeFe] and [NiFe] hydrogenases. This Perspective begins with a focus on the catalytic H-cluster of [FeFe] hydrogenase, which is highly active in producing molecular H 2 . There has been much recent progress in characterizing the enzyme-catalysed assembly of the H-cluster, including information gleaned from spectroscopy combined with in vitro isotopic labelling of this cluster using chemical synthesis. We then compare the lessons learned from H-cluster biosynthesis to what is known about the bioassembly of the binuclear active site of [NiFe] hydrogenase and the nitrogenase active site cluster FeMoco. Iron–sulfur enzymes catalyse multielectron redox reactions in nature. This Perspective describes the in vitro methodologies by which we study these enzyme biosyntheses and compares the way in which different active sites are constructed.