A Comparative, Two-Dimensional 14N ESEEM Characterization of Reduced [2Fe-2S] Clusters in Hyperthermophilic Archaeal High- and Low-Potential Rieske-Type Proteins Научная публикация
| Журнал |
Journal of Biological Inorganic Chemistry
ISSN: 0949-8257 , E-ISSN: 1432-1327 |
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| Вых. Данные | Год: 2004, Том: 9, Номер: 6, Страницы: 753-767 Страниц : 15 DOI: 10.1007/s00775-004-0571-y | ||||||||
| Ключевые слова | Archaea, Electron-spin echo envelope modulation (ESEEM), Hyperfine sublevel correlation (HYSCORE), Reduced [2Fe-2S] cluster, Rieske protein | ||||||||
| Авторы |
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| Организации |
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Информация о финансировании (6)
| 1 | National Science Foundation | 9910113 |
| 2 | National Institutes of Health | GM 62954 |
| 3 | National Institutes of Health | S10-RR15878 |
| 4 | Совет по грантам Президента Российской Федерации | НШ-1140.2003.3 |
| 5 | Japan Society for the Promotion of Science | BSAR-507 |
| 6 | Ministry of Education, Culture, Sports, Science and Technology | 11169237 |
Реферат:
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.
Библиографическая ссылка:
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 CAPlusCA 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 CAPlusCA OpenAlex
Даты:
| Поступила в редакцию: | 18 дек. 2003 г. |
| Принята к публикации: | 10 июн. 2004 г. |
| Опубликована online: | 8 июл. 2004 г. |
| Опубликована в печати: | 1 сент. 2004 г. |
Идентификаторы БД:
| Web of science: | WOS:000223956600013 |
| Scopus: | 2-s2.0-4644307317 |
| РИНЦ: | 13473433 |
| Chemical Abstracts: | 2004:725859 |
| Chemical Abstracts (print): | 141:362134 |
| OpenAlex: | W2129465699 |