Quantum refinement of [FeFe] hydrogenase indicates a dithiomethylamine ligand
(2010) In Journal of the American Chemical Society 132(13). p.4512-4512- Abstract
- The active site of the [FeFe] hydrogenases contains two Fe ions bound to one Cys ligand, three CO molecules, two CN(-) ions, and a dithiolate ligand. The nature of the last of these has been much discussed, and it has been suggested that it contains C, N, or O as the bridgehead atom. Most experimental studies indicate a N atom, whereas a recent density functional theory (DFT) study of a crystal structure indicated an O atom. Here, we performed quantum refinement on the same crystal structure with five different models of the dithiolate ligand X(CH(2)S(-))(2), with X = CH(2), NH(2)(+), NH (two conformations), or O; we found that structures with a N bridgehead atom actually provide the best fit to the raw crystallographic data. Quantum... (More)
- The active site of the [FeFe] hydrogenases contains two Fe ions bound to one Cys ligand, three CO molecules, two CN(-) ions, and a dithiolate ligand. The nature of the last of these has been much discussed, and it has been suggested that it contains C, N, or O as the bridgehead atom. Most experimental studies indicate a N atom, whereas a recent density functional theory (DFT) study of a crystal structure indicated an O atom. Here, we performed quantum refinement on the same crystal structure with five different models of the dithiolate ligand X(CH(2)S(-))(2), with X = CH(2), NH(2)(+), NH (two conformations), or O; we found that structures with a N bridgehead atom actually provide the best fit to the raw crystallographic data. Quantum refinement is standard crystallographic refinement in which the molecular mechanics force field normally used to supplement the experimental raw data to give a more chemical structure is replaced by more accurate DFT calculations for the active site. Thereby, we obtain structures that are an ideal compromise between DFT and crystallography. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1582149
- author
- Ryde, Ulf LU ; Greco, Claudio LU and De Gioia, Luca
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of the American Chemical Society
- volume
- 132
- issue
- 13
- pages
- 4512 - 4512
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000276553600005
- pmid:20230002
- scopus:77950818400
- pmid:20230002
- ISSN
- 1520-5126
- DOI
- 10.1021/ja909194f
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)
- id
- 1311e108-c3b7-472e-899d-516a732c15cd (old id 1582149)
- date added to LUP
- 2016-04-01 14:54:11
- date last changed
- 2023-02-07 02:35:08
@article{1311e108-c3b7-472e-899d-516a732c15cd, abstract = {{The active site of the [FeFe] hydrogenases contains two Fe ions bound to one Cys ligand, three CO molecules, two CN(-) ions, and a dithiolate ligand. The nature of the last of these has been much discussed, and it has been suggested that it contains C, N, or O as the bridgehead atom. Most experimental studies indicate a N atom, whereas a recent density functional theory (DFT) study of a crystal structure indicated an O atom. Here, we performed quantum refinement on the same crystal structure with five different models of the dithiolate ligand X(CH(2)S(-))(2), with X = CH(2), NH(2)(+), NH (two conformations), or O; we found that structures with a N bridgehead atom actually provide the best fit to the raw crystallographic data. Quantum refinement is standard crystallographic refinement in which the molecular mechanics force field normally used to supplement the experimental raw data to give a more chemical structure is replaced by more accurate DFT calculations for the active site. Thereby, we obtain structures that are an ideal compromise between DFT and crystallography.}}, author = {{Ryde, Ulf and Greco, Claudio and De Gioia, Luca}}, issn = {{1520-5126}}, language = {{eng}}, number = {{13}}, pages = {{4512--4512}}, publisher = {{The American Chemical Society (ACS)}}, series = {{Journal of the American Chemical Society}}, title = {{Quantum refinement of [FeFe] hydrogenase indicates a dithiomethylamine ligand}}, url = {{https://lup.lub.lu.se/search/files/136743482/136_fehase_cqx.pdf}}, doi = {{10.1021/ja909194f}}, volume = {{132}}, year = {{2010}}, }