X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase
Cosper, Nathaniel J. ; Stålhandske, Christina M. V. ; Saari, Ruth E. ; Hausinger, Robert P. ; Scott, R. A.
Springer
Published 1999
Springer
Published 1999
| ISSN: |
1432-1327
|
|---|---|
| Keywords: |
Key words α-Ketoglutarate dioxygenase ; TfdA ; X-ray absorption spectroscopy ; Extended X-ray absorption fine structure ; 2 ; 4-Dichlorophenoxyacetic acid
|
| Source: |
Springer Online Journal Archives 1860-2000
|
| Topics: |
Biology
Chemistry and Pharmacology
|
| Notes: |
Abstract The first step in the degradation of 2,4-dichlorophenoxyacetic acid (2,4-D) by Ralstonia eutropha JMP134 is catalyzed by the α-ketoglutarate (α-KG)-dependent dioxygenase TfdA. Previously, EPR and ESEEM studies on inactive Cu(II)-substituted TfdA suggested a mixture of nitrogen/oxygen coordination with two imidazole-like ligands. Differences between the spectra for Cu TfdA and α-KG- and 2,4-D-treated samples were interpreted as a rearrangement of the g–tensor principal axis system. Herein, we report the use of X-ray absorption spectroscopy (XAS) to further characterize the metal coordination environment of Cu TfdA as well as that in the active, wild-type Fe(II) enzyme. The EXAFS data are interpreted in terms of four N/O ligands (two imidazole-like) in the Cu TfdA sample and six N/O ligands (one or two imidazole-like) in the Fe TfdA sample. Addition of α-KG results in no significant structural change in coordination for Cu or Fe TfdA. However, addition of 2,4-D results in a decrease in the number of imidazole ligands in both Cu and Fe TfdA. Since this change is seen both in the Fe and Cu EXAFS, loss of one histidine ligand upon 2,4-D addition best describes the phenomenon. These XAS data clearly demonstrate that changes occur in the atomic environment of the metallocenter upon substrate binding.
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798295650495889408 |
|---|---|
| autor | Cosper, Nathaniel J. Stålhandske, Christina M. V. Saari, Ruth E. Hausinger, Robert P. Scott, R. A. |
| autorsonst | Cosper, Nathaniel J. Stålhandske, Christina M. V. Saari, Ruth E. Hausinger, Robert P. Scott, R. A. |
| book_url | http://dx.doi.org/10.1007/s007750050295 |
| datenlieferant | nat_lic_papers |
| hauptsatz | hsatz_simple |
| identnr | NLM206169493 |
| iqvoc_descriptor_title | iqvoc_00000708:analysis |
| issn | 1432-1327 |
| journal_name | JBIC |
| materialart | 1 |
| notes | Abstract The first step in the degradation of 2,4-dichlorophenoxyacetic acid (2,4-D) by Ralstonia eutropha JMP134 is catalyzed by the α-ketoglutarate (α-KG)-dependent dioxygenase TfdA. Previously, EPR and ESEEM studies on inactive Cu(II)-substituted TfdA suggested a mixture of nitrogen/oxygen coordination with two imidazole-like ligands. Differences between the spectra for Cu TfdA and α-KG- and 2,4-D-treated samples were interpreted as a rearrangement of the g–tensor principal axis system. Herein, we report the use of X-ray absorption spectroscopy (XAS) to further characterize the metal coordination environment of Cu TfdA as well as that in the active, wild-type Fe(II) enzyme. The EXAFS data are interpreted in terms of four N/O ligands (two imidazole-like) in the Cu TfdA sample and six N/O ligands (one or two imidazole-like) in the Fe TfdA sample. Addition of α-KG results in no significant structural change in coordination for Cu or Fe TfdA. However, addition of 2,4-D results in a decrease in the number of imidazole ligands in both Cu and Fe TfdA. Since this change is seen both in the Fe and Cu EXAFS, loss of one histidine ligand upon 2,4-D addition best describes the phenomenon. These XAS data clearly demonstrate that changes occur in the atomic environment of the metallocenter upon substrate binding. |
| package_name | Springer |
| publikationsjahr_anzeige | 1999 |
| publikationsjahr_facette | 1999 |
| publikationsjahr_intervall | 8004:1995-1999 |
| publikationsjahr_sort | 1999 |
| publisher | Springer |
| reference | 4 (1999), S. 122-129 |
| schlagwort | Key words α-Ketoglutarate dioxygenase TfdA X-ray absorption spectroscopy Extended X-ray absorption fine structure 2 4-Dichlorophenoxyacetic acid |
| search_space | articles |
| shingle_author_1 | Cosper, Nathaniel J. Stålhandske, Christina M. V. Saari, Ruth E. Hausinger, Robert P. Scott, R. A. |
| shingle_author_2 | Cosper, Nathaniel J. Stålhandske, Christina M. V. Saari, Ruth E. Hausinger, Robert P. Scott, R. A. |
| shingle_author_3 | Cosper, Nathaniel J. Stålhandske, Christina M. V. Saari, Ruth E. Hausinger, Robert P. Scott, R. A. |
| shingle_author_4 | Cosper, Nathaniel J. Stålhandske, Christina M. V. Saari, Ruth E. Hausinger, Robert P. Scott, R. A. |
| shingle_catch_all_1 | Cosper, Nathaniel J. Stålhandske, Christina M. V. Saari, Ruth E. Hausinger, Robert P. Scott, R. A. X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase Key words α-Ketoglutarate dioxygenase TfdA X-ray absorption spectroscopy Extended X-ray absorption fine structure 2 4-Dichlorophenoxyacetic acid Key words α-Ketoglutarate dioxygenase TfdA X-ray absorption spectroscopy Extended X-ray absorption fine structure 2 4-Dichlorophenoxyacetic acid Abstract The first step in the degradation of 2,4-dichlorophenoxyacetic acid (2,4-D) by Ralstonia eutropha JMP134 is catalyzed by the α-ketoglutarate (α-KG)-dependent dioxygenase TfdA. Previously, EPR and ESEEM studies on inactive Cu(II)-substituted TfdA suggested a mixture of nitrogen/oxygen coordination with two imidazole-like ligands. Differences between the spectra for Cu TfdA and α-KG- and 2,4-D-treated samples were interpreted as a rearrangement of the g–tensor principal axis system. Herein, we report the use of X-ray absorption spectroscopy (XAS) to further characterize the metal coordination environment of Cu TfdA as well as that in the active, wild-type Fe(II) enzyme. The EXAFS data are interpreted in terms of four N/O ligands (two imidazole-like) in the Cu TfdA sample and six N/O ligands (one or two imidazole-like) in the Fe TfdA sample. Addition of α-KG results in no significant structural change in coordination for Cu or Fe TfdA. However, addition of 2,4-D results in a decrease in the number of imidazole ligands in both Cu and Fe TfdA. Since this change is seen both in the Fe and Cu EXAFS, loss of one histidine ligand upon 2,4-D addition best describes the phenomenon. These XAS data clearly demonstrate that changes occur in the atomic environment of the metallocenter upon substrate binding. 1432-1327 14321327 Springer |
| shingle_catch_all_2 | Cosper, Nathaniel J. Stålhandske, Christina M. V. Saari, Ruth E. Hausinger, Robert P. Scott, R. A. X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase Key words α-Ketoglutarate dioxygenase TfdA X-ray absorption spectroscopy Extended X-ray absorption fine structure 2 4-Dichlorophenoxyacetic acid Key words α-Ketoglutarate dioxygenase TfdA X-ray absorption spectroscopy Extended X-ray absorption fine structure 2 4-Dichlorophenoxyacetic acid Abstract The first step in the degradation of 2,4-dichlorophenoxyacetic acid (2,4-D) by Ralstonia eutropha JMP134 is catalyzed by the α-ketoglutarate (α-KG)-dependent dioxygenase TfdA. Previously, EPR and ESEEM studies on inactive Cu(II)-substituted TfdA suggested a mixture of nitrogen/oxygen coordination with two imidazole-like ligands. Differences between the spectra for Cu TfdA and α-KG- and 2,4-D-treated samples were interpreted as a rearrangement of the g–tensor principal axis system. Herein, we report the use of X-ray absorption spectroscopy (XAS) to further characterize the metal coordination environment of Cu TfdA as well as that in the active, wild-type Fe(II) enzyme. The EXAFS data are interpreted in terms of four N/O ligands (two imidazole-like) in the Cu TfdA sample and six N/O ligands (one or two imidazole-like) in the Fe TfdA sample. Addition of α-KG results in no significant structural change in coordination for Cu or Fe TfdA. However, addition of 2,4-D results in a decrease in the number of imidazole ligands in both Cu and Fe TfdA. Since this change is seen both in the Fe and Cu EXAFS, loss of one histidine ligand upon 2,4-D addition best describes the phenomenon. These XAS data clearly demonstrate that changes occur in the atomic environment of the metallocenter upon substrate binding. 1432-1327 14321327 Springer |
| shingle_catch_all_3 | Cosper, Nathaniel J. Stålhandske, Christina M. V. Saari, Ruth E. Hausinger, Robert P. Scott, R. A. X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase Key words α-Ketoglutarate dioxygenase TfdA X-ray absorption spectroscopy Extended X-ray absorption fine structure 2 4-Dichlorophenoxyacetic acid Key words α-Ketoglutarate dioxygenase TfdA X-ray absorption spectroscopy Extended X-ray absorption fine structure 2 4-Dichlorophenoxyacetic acid Abstract The first step in the degradation of 2,4-dichlorophenoxyacetic acid (2,4-D) by Ralstonia eutropha JMP134 is catalyzed by the α-ketoglutarate (α-KG)-dependent dioxygenase TfdA. Previously, EPR and ESEEM studies on inactive Cu(II)-substituted TfdA suggested a mixture of nitrogen/oxygen coordination with two imidazole-like ligands. Differences between the spectra for Cu TfdA and α-KG- and 2,4-D-treated samples were interpreted as a rearrangement of the g–tensor principal axis system. Herein, we report the use of X-ray absorption spectroscopy (XAS) to further characterize the metal coordination environment of Cu TfdA as well as that in the active, wild-type Fe(II) enzyme. The EXAFS data are interpreted in terms of four N/O ligands (two imidazole-like) in the Cu TfdA sample and six N/O ligands (one or two imidazole-like) in the Fe TfdA sample. Addition of α-KG results in no significant structural change in coordination for Cu or Fe TfdA. However, addition of 2,4-D results in a decrease in the number of imidazole ligands in both Cu and Fe TfdA. Since this change is seen both in the Fe and Cu EXAFS, loss of one histidine ligand upon 2,4-D addition best describes the phenomenon. These XAS data clearly demonstrate that changes occur in the atomic environment of the metallocenter upon substrate binding. 1432-1327 14321327 Springer |
| shingle_catch_all_4 | Cosper, Nathaniel J. Stålhandske, Christina M. V. Saari, Ruth E. Hausinger, Robert P. Scott, R. A. X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase Key words α-Ketoglutarate dioxygenase TfdA X-ray absorption spectroscopy Extended X-ray absorption fine structure 2 4-Dichlorophenoxyacetic acid Key words α-Ketoglutarate dioxygenase TfdA X-ray absorption spectroscopy Extended X-ray absorption fine structure 2 4-Dichlorophenoxyacetic acid Abstract The first step in the degradation of 2,4-dichlorophenoxyacetic acid (2,4-D) by Ralstonia eutropha JMP134 is catalyzed by the α-ketoglutarate (α-KG)-dependent dioxygenase TfdA. Previously, EPR and ESEEM studies on inactive Cu(II)-substituted TfdA suggested a mixture of nitrogen/oxygen coordination with two imidazole-like ligands. Differences between the spectra for Cu TfdA and α-KG- and 2,4-D-treated samples were interpreted as a rearrangement of the g–tensor principal axis system. Herein, we report the use of X-ray absorption spectroscopy (XAS) to further characterize the metal coordination environment of Cu TfdA as well as that in the active, wild-type Fe(II) enzyme. The EXAFS data are interpreted in terms of four N/O ligands (two imidazole-like) in the Cu TfdA sample and six N/O ligands (one or two imidazole-like) in the Fe TfdA sample. Addition of α-KG results in no significant structural change in coordination for Cu or Fe TfdA. However, addition of 2,4-D results in a decrease in the number of imidazole ligands in both Cu and Fe TfdA. Since this change is seen both in the Fe and Cu EXAFS, loss of one histidine ligand upon 2,4-D addition best describes the phenomenon. These XAS data clearly demonstrate that changes occur in the atomic environment of the metallocenter upon substrate binding. 1432-1327 14321327 Springer |
| shingle_title_1 | X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase |
| shingle_title_2 | X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase |
| shingle_title_3 | X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase |
| shingle_title_4 | X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Springer Online Journal Archives 1860-2000 |
| timestamp | 2024-05-06T09:39:34.600Z |
| titel | X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase |
| titel_suche | X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase |
| topic | W V |
| uid | nat_lic_papers_NLM206169493 |