6j1h › Citations

Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase.

Fig. 1
Fig. 2
Fig. 3
Muraki N, Ishii K, Uchiyama S, Itoh SG, Okumura H, Aono S
OpenAccess logo Commun Biol 2 385 (2019)
Related entries: 6j0p, 6j1e, 6j1f, 6j1g, 6j1i, 6j1j

Cited: 4 times
EuropePMC logo PMID: 31646188

Abstract

Several accessory proteins are required for the assembly of the metal centers in hydrogenases. In NiFe-hydrogenases, CO and CN- are coordinated to the Fe in the NiFe dinuclear cluster of the active center. Though these diatomic ligands are biosynthesized enzymatically, detail mechanisms of their biosynthesis remain unclear. Here, we report the structural characterization of HypX responsible for CO biosynthesis to assemble the active site of NiFe hydrogenase. CoA is constitutionally bound in HypX. Structural characterization of HypX suggests that the formyl-group transfer will take place from N10-formyl-THF to CoA to form formyl-CoA in the N-terminal domain of HypX, followed by decarbonylation of formyl-CoA to produce CO in the C-terminal domain though the direct experimental results are not available yet. The conformation of CoA accommodated in the continuous cavity connecting the N- and C-terminal domains will interconvert between the extended and the folded conformations for HypX catalysis.

Articles - 6j1h mentioned but not cited (1)

  1. Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase. Muraki N, Ishii K, Uchiyama S, Itoh SG, Okumura H, Aono S. Commun Biol 2 385 (2019)


Reviews citing this publication (1)

  1. Biophysical research in Okazaki, Japan. Akiyama S, Aoki K, Kubo Y. Biophys Rev 12 237-243 (2020)

Articles citing this publication (2)

  1. In Vitro Biosynthesis of the [Fe]-Hydrogenase Cofactor Verifies the Proposed Biosynthetic Precursors. Schaupp S, Arriaza-Gallardo FJ, Pan HJ, Kahnt J, Angelidou G, Paczia N, Costa K, Hu X, Shima S. Angew Chem Int Ed Engl 61 e202200994 (2022)
  2. Elucidating polymorphs of crystal structures by intensity-based hierarchical clustering analysis of multiple diffraction data sets. Matsuura H, Sakai N, Toma-Fukai S, Muraki N, Hayama K, Kamikubo H, Aono S, Kawano Y, Yamamoto M, Hirata K. Acta Crystallogr D Struct Biol 79 909-924 (2023)


Quick links