A Comparative, Two-Dimensional 14N ESEEM Characterization of Reduced [2Fe-2S] Clusters in Hyperthermophilic Archaeal High- and Low-Potential Rieske-Type Proteins Full article
| Journal |
Journal of Biological Inorganic Chemistry
ISSN: 0949-8257 , E-ISSN: 1432-1327 |
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| Output data | Year: 2004, Volume: 9, Number: 6, Pages: 753-767 Pages count : 15 DOI: 10.1007/s00775-004-0571-y | ||||||||
| Tags | Archaea, Electron-spin echo envelope modulation (ESEEM), Hyperfine sublevel correlation (HYSCORE), Reduced [2Fe-2S] cluster, Rieske protein | ||||||||
| Authors |
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| Affiliations |
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Funding (6)
| 1 | National Science Foundation | 9910113 |
| 2 | National Institutes of Health | GM 62954 |
| 3 | National Institutes of Health | S10-RR15878 |
| 4 | Council for Grants of the President of the Russian Federation | НШ-1140.2003.3 |
| 5 | Japan Society for the Promotion of Science | BSAR-507 |
| 6 | Ministry of Education, Culture, Sports, Science and Technology | 11169237 |
Abstract:
Proteins of the Rieske and Rieske-type family contain a [2Fe–2S] cluster with mixed ligation by two histidines and two cysteines, and play important roles in various biological electron transfer reactions. We report here the comparative orientation-selected ESEEM and HYSCORE studies of the reduced clusters from two hyperthermophilic Rieske-type proteins; a high-potential, archaeal Rieske protein called sulredoxin (SDX) from Sulfolobus tokodaii with weak homology to the cytochrome bc-associated Rieske proteins, and a low-potential, archaeal homolog of an oxygenase-associated Rieske-type ferredoxin (ARF) from Sulfolobus solfataricus. 14N ESEEM and HYSCORE spectra of SDX and ARF show well-defined variations, which are primarily determined by changes of quadrupole couplings (up to 50% depending on the selected orientation) of the two coordinated nitrogens. These are due to variations in coordination geometry of the histidine imidazole ligands rather than to variations of hyperfine couplings of these nitrogens, which do not exceed 8–10%. The measured quadrupole couplings and their differences in the two proteins are consistent with those calculated using the reported crystal structures of high- and low-potential Rieske proteins. These results suggest that exploration of quadrupole tensors might provide a more accurate method for characterization of the histidine coordination in different proteins and mutants than hyperfine tensors, and might have potential applications in a wider range of biological systems.
Cite:
Dikanov S.A.
, Shubin A.A.
, Kounosu A.
, Iwasaki T.
, Samoilova R.I.
A Comparative, Two-Dimensional 14N ESEEM Characterization of Reduced [2Fe-2S] Clusters in Hyperthermophilic Archaeal High- and Low-Potential Rieske-Type Proteins
Journal of Biological Inorganic Chemistry. 2004. V.9. N6. P.753-767. DOI: 10.1007/s00775-004-0571-y WOS Scopus РИНЦ ANCAN OpenAlex
A Comparative, Two-Dimensional 14N ESEEM Characterization of Reduced [2Fe-2S] Clusters in Hyperthermophilic Archaeal High- and Low-Potential Rieske-Type Proteins
Journal of Biological Inorganic Chemistry. 2004. V.9. N6. P.753-767. DOI: 10.1007/s00775-004-0571-y WOS Scopus РИНЦ ANCAN OpenAlex
Dates:
| Submitted: | Dec 18, 2003 |
| Accepted: | Jun 10, 2004 |
| Published online: | Jul 8, 2004 |
| Published print: | Sep 1, 2004 |
Identifiers:
| Web of science: | WOS:000223956600013 |
| Scopus: | 2-s2.0-4644307317 |
| Elibrary: | 13473433 |
| Chemical Abstracts: | 2004:725859 |
| Chemical Abstracts (print): | 141:362134 |
| OpenAlex: | W2129465699 |