| Sequential resonance assignments of oxidized high-potential iron-sulfur protein from Chromatium vinosum. | |
| | |
MedLine Citation:
|
PMID: 1734968 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
2D NMR spectra of the high-potential iron-sulfur protein (HiPIP) from Chromatium vinosum have been used to obtain partial resonance assignments for the oxidized paramagnetic redox state of the protein. Sequence-specific assignments were made using NOESY and COSY spectra in H2O and D2O of the following backbone segments: Asn-5-Arg-33, Glu-39-Asp-45, Gly-55-Cys-63, Gly-68-Ala-78, and Leu-82-Gly-85. NOESY spectra with a spectral width wide enough to include the hyperfine-shifted resonances revealed numerous NOE contacts between these signals and those in the main envelope of the proton spectrum. With the aid of the X-ray crystal structure [Carter, C.W., Kraut, J., Freer, S. T., Xuong, N. H., Alden, R. A., & Bartsch, R. G. (1974) J. Biol. Chem. 249, 4212], these NOEs permitted seven of the nine hyperfine-shifted signals to be assigned to three of the cysteine residues liganded to the metal cluster (Cys-43, Cys-46, and Cys-77). The other two hyperfine-shifted signals produced no detectable NOEs to other resonances in the spectrum and were tentatively assigned to the remaining cysteinyl ligand (Cys-63). These assignments, in conjunction with recent theoretical models of the electronic structure of the Fe4S4 cluster [Noodleman, L. (1988) Inorg. Chem. 27, 3677; Bertini, I., Briganti, F., Luchinat, C., Scozzafava, A., & Sola, M. (1991) J. Am. Chem. Soc. 113, 1237], indicate that the iron atoms coordinated to Cys-63 and Cys-77 are those of the mixed-valence Fe(3+)-Fe2+ pair whereas Cys-43 and Cys-46 are ligands to the Fe(3+)-Fe3+ metal pair. |
| | |
Authors:
|
D G Nettesheim; S R Harder; B A Feinberg; J D Otvos |
Related Documents
:
|
8851748 - Spectral characterization of fluconazole. 17549778 - 1h and 13c-nmr data of hydroxyflavone derivatives. 22905018 - 2,7-dimeth-oxy-1-(2-naphtho-yl)naph-thalene. 9390408 - Tritium nmr studies of the human carbonic anhydrase i-benzenesulfonamide complex. 21353348 - Pyridine-derived thiosemicarbazones and their tin(iv) complexes with antifungal activit... 16791498 - Ct-operated bifunctional fluorescent probe based on a pretwisted donor-donor-biphenyl. |
Publication Detail:
|
Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
|
Title: Biochemistry Volume: 31 ISSN: 0006-2960 ISO Abbreviation: Biochemistry Publication Date: 1992 Feb |
Date Detail:
|
Created Date: 1992-03-06 Completed Date: 1992-03-06 Revised Date: 2007-11-14 |
Medline Journal Info:
|
Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: UNITED STATES |
Other Details:
|
Languages: eng Pagination: 1234-44 Citation Subset: IM |
Affiliation:
|
Department of Chemistry, University of Wisconsin-Milwaukee 53201. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Amino Acid Sequence Bacterial Proteins / chemistry Chromatium / chemistry* Cysteine / chemistry Iron-Sulfur Proteins / chemistry* Magnetic Resonance Spectroscopy Molecular Sequence Data Oxidation-Reduction Peptides / chemistry Protein Conformation Tryptophan / chemistry Tyrosine / chemistry |
| Grant Support | |
ID/Acronym/Agency:
|
GM 41927-01/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
|
0/Bacterial Proteins; 0/Iron-Sulfur Proteins; 0/Peptides; 52-90-4/Cysteine; 55520-40-6/Tyrosine; 73-22-3/Tryptophan |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Posttranslational modification of Klebsiella pneumoniae flavodoxin by covalent attachment of coenzym...
Next Document: Sequence-specific 1H NMR assignments and solution structure of bovine pancreatic polypeptide.