Ligand binding at the A-cluster in full-length or truncated acetyl-CoA synthase studied by X-ray absorption spectroscopy.
Bacteria integrate CO2 reduction and acetyl coenzyme-A (CoA) synthesis in the Wood-Ljungdal pathway. The acetyl-CoA synthase (ACS) active site is a [4Fe4S]-[NiNi] complex (A-cluster). The dinickel site structure (with proximal, p, and distal, d, ions) was studied by X-ray absorption spectroscopy in...
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Public Library of Science (PLoS)
2017-01-01
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| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0171039&type=printable |
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| author | Peer Schrapers Julia Ilina Christina M Gregg Stefan Mebs Jae-Hun Jeoung Holger Dau Holger Dobbek Michael Haumann |
| author_facet | Peer Schrapers Julia Ilina Christina M Gregg Stefan Mebs Jae-Hun Jeoung Holger Dau Holger Dobbek Michael Haumann |
| author_sort | Peer Schrapers |
| collection | DOAJ |
| description | Bacteria integrate CO2 reduction and acetyl coenzyme-A (CoA) synthesis in the Wood-Ljungdal pathway. The acetyl-CoA synthase (ACS) active site is a [4Fe4S]-[NiNi] complex (A-cluster). The dinickel site structure (with proximal, p, and distal, d, ions) was studied by X-ray absorption spectroscopy in ACS variants comprising all three protein domains or only the C-terminal domain with the A-cluster. Both variants showed two square-planar Ni(II) sites and an OH- bound at Ni(II)p in oxidized enzyme and a H2O at Ni(I)p in reduced enzyme; a Ni(I)p-CO species was induced by CO incubation and a Ni(II)-CH3- species with an additional water ligand by a methyl group donor. These findings render a direct effect of the N-terminal and middle domains on the A-cluster structure unlikely. |
| format | Article |
| id | doaj-art-703ef1f0bf3845a4862a5bf790ef31d5 |
| institution | DOAJ |
| issn | 1932-6203 |
| language | English |
| publishDate | 2017-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj-art-703ef1f0bf3845a4862a5bf790ef31d52025-08-20T03:04:34ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01122e017103910.1371/journal.pone.0171039Ligand binding at the A-cluster in full-length or truncated acetyl-CoA synthase studied by X-ray absorption spectroscopy.Peer SchrapersJulia IlinaChristina M GreggStefan MebsJae-Hun JeoungHolger DauHolger DobbekMichael HaumannBacteria integrate CO2 reduction and acetyl coenzyme-A (CoA) synthesis in the Wood-Ljungdal pathway. The acetyl-CoA synthase (ACS) active site is a [4Fe4S]-[NiNi] complex (A-cluster). The dinickel site structure (with proximal, p, and distal, d, ions) was studied by X-ray absorption spectroscopy in ACS variants comprising all three protein domains or only the C-terminal domain with the A-cluster. Both variants showed two square-planar Ni(II) sites and an OH- bound at Ni(II)p in oxidized enzyme and a H2O at Ni(I)p in reduced enzyme; a Ni(I)p-CO species was induced by CO incubation and a Ni(II)-CH3- species with an additional water ligand by a methyl group donor. These findings render a direct effect of the N-terminal and middle domains on the A-cluster structure unlikely.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0171039&type=printable |
| spellingShingle | Peer Schrapers Julia Ilina Christina M Gregg Stefan Mebs Jae-Hun Jeoung Holger Dau Holger Dobbek Michael Haumann Ligand binding at the A-cluster in full-length or truncated acetyl-CoA synthase studied by X-ray absorption spectroscopy. PLoS ONE |
| title | Ligand binding at the A-cluster in full-length or truncated acetyl-CoA synthase studied by X-ray absorption spectroscopy. |
| title_full | Ligand binding at the A-cluster in full-length or truncated acetyl-CoA synthase studied by X-ray absorption spectroscopy. |
| title_fullStr | Ligand binding at the A-cluster in full-length or truncated acetyl-CoA synthase studied by X-ray absorption spectroscopy. |
| title_full_unstemmed | Ligand binding at the A-cluster in full-length or truncated acetyl-CoA synthase studied by X-ray absorption spectroscopy. |
| title_short | Ligand binding at the A-cluster in full-length or truncated acetyl-CoA synthase studied by X-ray absorption spectroscopy. |
| title_sort | ligand binding at the a cluster in full length or truncated acetyl coa synthase studied by x ray absorption spectroscopy |
| url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0171039&type=printable |
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