Reconstitution of 3-Acetyl Chlorophyll <i>a</i> into Light-Harvesting Complex 2 from the Purple Photosynthetic Bacterium <i>Phaeospirillum molischianum</i>
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- Yoshitaka Saga
- Department of Chemistry, Faculty of Science and Engineering, Kindai University, Higashi-Osaka 577-8502, Osaka, Japan
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- Madoka Yamashita
- Department of Chemistry, Faculty of Science and Engineering, Kindai University, Higashi-Osaka 577-8502, Osaka, Japan
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- Michie Imanishi
- Graduate School of Agricultural Science, Kobe University, Kobe 657-8501, Japan
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- Yukihiro Kimura
- Graduate School of Agricultural Science, Kobe University, Kobe 657-8501, Japan
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- Yuto Masaoka
- Graduate School of Life Sciences, Ritsumeikan University, Kusatsu 525-8577, Shiga, Japan
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- Tsubasa Hidaka
- Graduate School of Life Sciences, Ritsumeikan University, Kusatsu 525-8577, Shiga, Japan
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- Yutaka Nagasawa
- Graduate School of Life Sciences, Ritsumeikan University, Kusatsu 525-8577, Shiga, Japan
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説明
[Image: see text] The manipulation of B800 bacteriochlorophyll (BChl) a in light-harvesting complex 2 (LH2) from the purple photosynthetic bacterium Phaeospirillum molischianum (molischianum-LH2) provides insight for understanding the energy transfer mechanism and the binding of cyclic tetrapyrroles in LH2 proteins since molischianum-LH2 is one of the two LH2 proteins whose atomic-resolution structures have been determined and is a representative of type-2 LH2 proteins. However, there is no report on the substitution of B800 BChl a in molischianum-LH2. We report the reconstitution of 3-acetyl chlorophyll (AcChl) a, which has a 17,18-dihydroporphyrin skeleton, to the B800 site in molischianum-LH2. The 3-acetyl group in AcChl a formed a hydrogen bond with β′-Thr23 in essentially the same manner as native B800 BChl a, but this hydrogen bond was weaker than that of B800 BChl a. This change can be rationalized by invoking a small distortion in the orientation of the 3-acetyl group in the B800 cavity by dehydrogenation in the B-ring from BChl a. The energy transfer from AcChl a in the B800 site to B850 BChl a was about 5-fold slower than that from native B800 BChl a by a decrease of the spectral overlap between energy-donating AcChl a and energy-accepting B850 BChl a.
収録刊行物
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- ACS Omega
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ACS Omega 5 (12), 6817-6825, 2020-03-18
American Chemical Society (ACS)
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詳細情報 詳細情報について
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- CRID
- 1360286992998798336
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- ISSN
- 24701343
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- 資料種別
- journal article
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- データソース種別
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- Crossref
- KAKEN
- OpenAIRE
