دورية أكاديمية
Interaction of photosystem I-derived protons with the water-splitting enzyme complex. Evidence for localized domains.
| العنوان: | Interaction of photosystem I-derived protons with the water-splitting enzyme complex. Evidence for localized domains. |
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| المؤلفون: | Theg SM, Belanger KM, Dilley RA |
| المصدر: | Journal of bioenergetics and biomembranes [J Bioenerg Biomembr] 1987 Feb; Vol. 19 (1), pp. 53-68. |
| نوع المنشور: | Journal Article; Research Support, U.S. Gov't, Non-P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: Springer Country of Publication: United States NLM ID: 7701859 Publication Model: Print Cited Medium: Print ISSN: 0145-479X (Print) Linking ISSN: 0145479X NLM ISO Abbreviation: J Bioenerg Biomembr Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 1999- : New York, NY : Springer Original Publication: New York, Plenum Press. |
| مواضيع طبية MeSH: | Protons*, Chlorophyll/*metabolism , Oxidoreductases/*metabolism , Plant Proteins/*metabolism, Dicyclohexylcarbodiimide/pharmacology ; Electron Transport/drug effects ; Fluorescence ; Kinetics ; Light-Harvesting Protein Complexes ; Organotin Compounds/pharmacology ; Oxygen/biosynthesis ; Photosynthetic Reaction Center Complex Proteins ; Photosystem I Protein Complex ; Photosystem II Protein Complex ; Time Factors |
| مستخلص: | The induction of millisecond delayed fluorescence mediated by PS I-dependent proton pumping has been used as an indicator of the time course with which those protons equilibrate with sites on the oxygen-evolving enzyme complex (Bowes, J. M., and Crofts, A. R. (1978). Z. Naturforsch. 33C, 271-275). We found that the induction curves were retarded by a reversible exposure of non-energized thylakoids to low concentrations of the uncoupler, desaspidin, at alkaline, but not at neutral, pH. The induction curves were not retarded by increasing the buffering capacity of the thylakoid lumen with Tricine, and were inhibited by the energy transfer inhibitors, dicyclohexylcarbodiimide (DCCD) and triphenyltin chloride (TPT). These data suggest that the catalytic site of the water-splitting complex is located in proton-sequestering membrane domains, rather than at the lumen-exposed inner membrane surface, protons released during PS I-mediated electron transport might equilibrate with protonatable sites on the oxygen-evolving complex without passing through the lumen, and those protons may travel over specific conducting pathways which can be blocked by DCCD and TPT. |
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| المشرفين على المادة: | 0 (Light-Harvesting Protein Complexes) 0 (Organotin Compounds) 0 (Photosynthetic Reaction Center Complex Proteins) 0 (Photosystem I Protein Complex) 0 (Photosystem II Protein Complex) 0 (Plant Proteins) 0 (Protons) 1406-65-1 (Chlorophyll) 538-75-0 (Dicyclohexylcarbodiimide) EC 1.- (Oxidoreductases) I1L80IDY27 (triphenyltin chloride) S88TT14065 (Oxygen) |
| تواريخ الأحداث: | Date Created: 19870201 Date Completed: 19870618 Latest Revision: 20190919 |
| رمز التحديث: | 20221208 |
| DOI: | 10.1007/BF00769732 |
| PMID: | 3032930 |
| قاعدة البيانات: | MEDLINE |
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Full Text Finder | تدمد: | 0145-479X |
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| DOI: | 10.1007/BF00769732 |