Nitrogenase assembly

Abstract

Nitrogenase contains two unique metalloclusters: the P-cluster and the M-cluster. The assembly processes of P- and M-clusters are arguably the most complicated processes in bioinorganic chemistry. There is considerable interest in decoding the biosynthetic mechanisms of the P- and M-clusters, because these clusters are not only biologically important, but also chemically unprecedented. Understanding the assembly mechanisms of these unique metalloclusters is crucial for understanding the structure-function relationship of nitrogenase. Here, we review the recent advances in this research area, with an emphasis on our work that provide important insights into the biosynthetic pathways of these high-nuclearity metal centers. This article is part of a Special Issue entitled: Metals in Bioenergetics and Biomimetics Systems.

Keywords: 5’-dA; 5′-deoxyadenosine; ADP; ATP; Assembly; EPR; EXAFS; HPLC; IDS; M-cluster; MCD; MS; Metallocluster; MoO(4)(2-); Nitrogenase; P-cluster; S-adenosyl-homocysteine; S-adenosyl-methionine; SAH; SAM; SAXS; XAS; adenosine diphosphate; adenosine triphosphate; electron paramagnetic resonance; extended x-ray absorption fine structure; high performance liquid chromatography; indigo disulfonate; magnetic circular dichroism; mass spectrometry; molybdate; small angle x-ray scattering; x-ray absorption spectroscopy.