Chemical rescue of a site-modified ligand to a [4Fe–4S] cluster in PsaC, a bacterial-like dicluster ferredoxin bound to Photosystem I
Chemical rescue of site-modified amino acids using externally supplied organic molecules represents a powerful method to investigate structure–function relationships in proteins. Here we provide definitive evidence that aryl and alkyl thiolates, reagents typically used for in vitro iron–sulfur clust...
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| Published in: | Biochimica et biophysica acta Vol. 1767; no. 6; pp. 712 - 724 |
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| Main Authors: | , , , , , , , , , |
| Format: | Journal Article |
| Language: | English |
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Elsevier B.V
01-06-2007
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| Abstract | Chemical rescue of site-modified amino acids using externally supplied organic molecules represents a powerful method to investigate structure–function relationships in proteins. Here we provide definitive evidence that aryl and alkyl thiolates, reagents typically used for
in vitro iron–sulfur cluster reconstitutions, serve as rescue ligands to a site-specifically modified [4Fe–4S]
1+,2+ cluster in PsaC, a bacterial dicluster ferredoxin-like subunit of Photosystem I. PsaC binds two low-potential [4Fe–4S]
1+,2+ clusters termed F
A and F
B. In the C13G/C33S variant of PsaC, glycine has replaced cysteine at position 13 creating a protein that is missing one of the ligating amino acids to iron–sulfur cluster F
B. Using a variety of analytical techniques, including non-heme iron and acid-labile sulfur assays, and EPR, resonance Raman, and Mössbauer spectroscopies, we showed that the C13G/C33S variant of PsaC binds two [4Fe–4S]
1+,2+ clusters, despite the absence of one of the biological ligands.
19F NMR spectroscopy indicated that the external thiolate replaces cysteine 13 as a substitute ligand to the F
B cluster. The finding that site-modified [4Fe–4S]
1+,2+ clusters can be chemically rescued with external thiolates opens new opportunities for modulating their properties in proteins. In particular, it provides a mechanism to attach an additional electron transfer cofactor to the protein
via a bound, external ligand. |
|---|---|
| AbstractList | Chemical rescue of site-modified amino acids using externally supplied organic molecules represents a powerful method to investigate structure-function relationships in proteins. Here we provide definitive evidence that aryl and alkyl thiolates, reagents typically used for in vitro iron-sulfur cluster reconstitutions, serve as rescue ligands to a site-specifically modified [4Fe-4S](1+,2+) cluster in PsaC, a bacterial dicluster ferredoxin-like subunit of Photosystem I. PsaC binds two low-potential [4Fe-4S](1+,2+) clusters termed F(A) and F(B). In the C13G/C33S variant of PsaC, glycine has replaced cysteine at position 13 creating a protein that is missing one of the ligating amino acids to iron-sulfur cluster F(B). Using a variety of analytical techniques, including non-heme iron and acid-labile sulfur assays, and EPR, resonance Raman, and Mössbauer spectroscopies, we showed that the C13G/C33S variant of PsaC binds two [4Fe-4S](1+,2+) clusters, despite the absence of one of the biological ligands. (19)F NMR spectroscopy indicated that the external thiolate replaces cysteine 13 as a substitute ligand to the F(B) cluster. The finding that site-modified [4Fe-4S](1+,2+) clusters can be chemically rescued with external thiolates opens new opportunities for modulating their properties in proteins. In particular, it provides a mechanism to attach an additional electron transfer cofactor to the protein via a bound, external ligand. Chemical rescue of site-modified amino acids using externally supplied organic molecules represents a powerful method to investigate structure–function relationships in proteins. Here we provide definitive evidence that aryl and alkyl thiolates, reagents typically used for in vitro iron–sulfur cluster reconstitutions, serve as rescue ligands to a site-specifically modified [4Fe–4S] 1+,2+ cluster in PsaC, a bacterial dicluster ferredoxin-like subunit of Photosystem I. PsaC binds two low-potential [4Fe–4S] 1+,2+ clusters termed F A and F B. In the C13G/C33S variant of PsaC, glycine has replaced cysteine at position 13 creating a protein that is missing one of the ligating amino acids to iron–sulfur cluster F B. Using a variety of analytical techniques, including non-heme iron and acid-labile sulfur assays, and EPR, resonance Raman, and Mössbauer spectroscopies, we showed that the C13G/C33S variant of PsaC binds two [4Fe–4S] 1+,2+ clusters, despite the absence of one of the biological ligands. 19F NMR spectroscopy indicated that the external thiolate replaces cysteine 13 as a substitute ligand to the F B cluster. The finding that site-modified [4Fe–4S] 1+,2+ clusters can be chemically rescued with external thiolates opens new opportunities for modulating their properties in proteins. In particular, it provides a mechanism to attach an additional electron transfer cofactor to the protein via a bound, external ligand. |
| Author | Maes, Estelle M. Falzone, Christopher J. Antonkine, Mikhail L. Breitenstein, Christoph Balasubramanian, Ramakrishnan Lubner, Carolyn Czernuszewicz, Roman S. Bill, Eckhard Golbeck, John H. Bryant, Donald A. |
| Author_xml | – sequence: 1 givenname: Mikhail L. surname: Antonkine fullname: Antonkine, Mikhail L. email: antonkin@physik.fu-berlin.de organization: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA – sequence: 2 givenname: Estelle M. surname: Maes fullname: Maes, Estelle M. organization: Department of Chemistry, University of Houston, Houston, TX 77204, USA – sequence: 3 givenname: Roman S. surname: Czernuszewicz fullname: Czernuszewicz, Roman S. organization: Department of Chemistry, University of Houston, Houston, TX 77204, USA – sequence: 4 givenname: Christoph surname: Breitenstein fullname: Breitenstein, Christoph organization: Max-Planck-Institut für Bioanorganische Chemie, Stiftstr. 34-36, Mülheim an der Ruhr, D-45470, Germany – sequence: 5 givenname: Eckhard surname: Bill fullname: Bill, Eckhard organization: Max-Planck-Institut für Bioanorganische Chemie, Stiftstr. 34-36, Mülheim an der Ruhr, D-45470, Germany – sequence: 6 givenname: Christopher J. surname: Falzone fullname: Falzone, Christopher J. organization: Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA – sequence: 7 givenname: Ramakrishnan surname: Balasubramanian fullname: Balasubramanian, Ramakrishnan organization: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA – sequence: 8 givenname: Carolyn surname: Lubner fullname: Lubner, Carolyn organization: Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA – sequence: 9 givenname: Donald A. surname: Bryant fullname: Bryant, Donald A. organization: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA – sequence: 10 givenname: John H. surname: Golbeck fullname: Golbeck, John H. organization: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17434441$$D View this record in MEDLINE/PubMed |
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| Keywords | S ≥ 3/2 Chemical rescue NMR PsaC [4Fe–4S] cluster EPR P700-F X core Photosystem I PS I F A and F B Iron–sulfur protein |
| Language | English |
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| Snippet | Chemical rescue of site-modified amino acids using externally supplied organic molecules represents a powerful method to investigate structure–function... Chemical rescue of site-modified amino acids using externally supplied organic molecules represents a powerful method to investigate structure-function... |
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| SubjectTerms | [4Fe–4S] cluster Chemical rescue Ferredoxins - metabolism Iron-Sulfur Proteins - chemistry Iron-Sulfur Proteins - metabolism Iron–sulfur protein Ligands Photosystem I Photosystem I Protein Complex - chemistry Photosystem I Protein Complex - metabolism PsaC S ≥ 3/2 |
| Title | Chemical rescue of a site-modified ligand to a [4Fe–4S] cluster in PsaC, a bacterial-like dicluster ferredoxin bound to Photosystem I |
| URI | https://dx.doi.org/10.1016/j.bbabio.2007.02.003 https://www.ncbi.nlm.nih.gov/pubmed/17434441 |
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