Structural insights into blue-green light utilization by marine green algal light harvesting complex II at 2.78 Å
Light-harvesting complex II (LHCII) present in plants and green algae absorbs solar energy to promote photochemical reactions. A marine green macroalga, Codium fragile, exhibits the unique characteristic of absorbing blue-green light from the sun during photochemical reactions while being underwater...
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| Format: | Article |
| Language: | English |
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Elsevier
2022-01-01
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| Series: | BBA Advances |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2667160322000242 |
| _version_ | 1797988220211822592 |
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| author | Soichiro Seki Tetsuko Nakaniwa Pablo Castro-Hartmann Kasim Sader Akihiro Kawamoto Hideaki Tanaka Pu Qian Genji Kurisu Ritsuko Fujii |
| author_facet | Soichiro Seki Tetsuko Nakaniwa Pablo Castro-Hartmann Kasim Sader Akihiro Kawamoto Hideaki Tanaka Pu Qian Genji Kurisu Ritsuko Fujii |
| author_sort | Soichiro Seki |
| collection | DOAJ |
| description | Light-harvesting complex II (LHCII) present in plants and green algae absorbs solar energy to promote photochemical reactions. A marine green macroalga, Codium fragile, exhibits the unique characteristic of absorbing blue-green light from the sun during photochemical reactions while being underwater owing to the presence of pigment-altered LHCII called siphonaxanthin–chlorophyll a/b-binding protein (SCP). In this study, we determined the structure of SCP at a resolution of 2.78 Å using cryogenic electron microscopy. SCP has a trimeric structure, wherein each monomer containing two lutein and two chlorophyll a molecules in the plant-type LHCII are replaced by siphonaxanthin and its ester and two chlorophyll b molecules, respectively. Siphonaxanthin occupies the binding site in SCP having a polarity in the trimeric inner core, and exhibits a distorted conjugated chain comprising a carbonyl group hydrogen bonded to a cysteine residue of apoprotein. These features suggest that the siphonaxanthin molecule is responsible for the characteristic green absorption of SCP. The replaced chlorophyll b molecules extend the region of the stromal side chlorophyll b cluster, spanning two adjacent monomers. |
| first_indexed | 2024-04-11T08:00:38Z |
| format | Article |
| id | doaj.art-abc6d70855554ef4801f3bf8324f77c3 |
| institution | Directory Open Access Journal |
| issn | 2667-1603 |
| language | English |
| last_indexed | 2024-04-11T08:00:38Z |
| publishDate | 2022-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | BBA Advances |
| spelling | doaj.art-abc6d70855554ef4801f3bf8324f77c32022-12-22T04:35:44ZengElsevierBBA Advances2667-16032022-01-012100064Structural insights into blue-green light utilization by marine green algal light harvesting complex II at 2.78 ÅSoichiro Seki0Tetsuko Nakaniwa1Pablo Castro-Hartmann2Kasim Sader3Akihiro Kawamoto4Hideaki Tanaka5Pu Qian6Genji Kurisu7Ritsuko Fujii8Division of Molecular Materials Science, Graduate School of Science, Osaka City University, 3-3-138, Sugimoto, Sumiyoshi-ku, Osaka 558–8585, JapanInstitute for Protein Research, Osaka University, Suita, Osaka 565–0871, JapanMaterials and Structural Analysis, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 GG Eindhoven, NetherlandsMaterials and Structural Analysis, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 GG Eindhoven, NetherlandsInstitute for Protein Research, Osaka University, Suita, Osaka 565–0871, Japan; Institute for Open and Transdisciplinary Research Initiatives (OTRI), Osaka University, Suita, Osaka 565–9871, JapanInstitute for Protein Research, Osaka University, Suita, Osaka 565–0871, Japan; Institute for Open and Transdisciplinary Research Initiatives (OTRI), Osaka University, Suita, Osaka 565–9871, JapanMaterials and Structural Analysis, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 GG Eindhoven, NetherlandsInstitute for Protein Research, Osaka University, Suita, Osaka 565–0871, Japan; Institute for Open and Transdisciplinary Research Initiatives (OTRI), Osaka University, Suita, Osaka 565–9871, JapanDivision of Molecular Materials Science, Graduate School of Science, Osaka City University, 3-3-138, Sugimoto, Sumiyoshi-ku, Osaka 558–8585, Japan; Department of Chemistry, Graduate School of Science, Osaka Metropolitan University, 3-3-138, Sugimoto, Sumiyoshi-ku, Osaka 558–8585, Japan; Research Center for Artificial Photosynthesis (ReCAP), Osaka Metropolitan University, 3-3-138, Sugimoto, Sumiyoshi-ku, Osaka 558–8585, Japan; Corresponding author.Light-harvesting complex II (LHCII) present in plants and green algae absorbs solar energy to promote photochemical reactions. A marine green macroalga, Codium fragile, exhibits the unique characteristic of absorbing blue-green light from the sun during photochemical reactions while being underwater owing to the presence of pigment-altered LHCII called siphonaxanthin–chlorophyll a/b-binding protein (SCP). In this study, we determined the structure of SCP at a resolution of 2.78 Å using cryogenic electron microscopy. SCP has a trimeric structure, wherein each monomer containing two lutein and two chlorophyll a molecules in the plant-type LHCII are replaced by siphonaxanthin and its ester and two chlorophyll b molecules, respectively. Siphonaxanthin occupies the binding site in SCP having a polarity in the trimeric inner core, and exhibits a distorted conjugated chain comprising a carbonyl group hydrogen bonded to a cysteine residue of apoprotein. These features suggest that the siphonaxanthin molecule is responsible for the characteristic green absorption of SCP. The replaced chlorophyll b molecules extend the region of the stromal side chlorophyll b cluster, spanning two adjacent monomers.http://www.sciencedirect.com/science/article/pii/S2667160322000242Codium fragileCryo-EMLight-harvesting complexSiphonaxanthin–chlorophyll a/b-binding protein (SCP)Intermonomer chlorophyll b macrocluster |
| spellingShingle | Soichiro Seki Tetsuko Nakaniwa Pablo Castro-Hartmann Kasim Sader Akihiro Kawamoto Hideaki Tanaka Pu Qian Genji Kurisu Ritsuko Fujii Structural insights into blue-green light utilization by marine green algal light harvesting complex II at 2.78 Å BBA Advances Codium fragile Cryo-EM Light-harvesting complex Siphonaxanthin–chlorophyll a/b-binding protein (SCP) Intermonomer chlorophyll b macrocluster |
| title | Structural insights into blue-green light utilization by marine green algal light harvesting complex II at 2.78 Å |
| title_full | Structural insights into blue-green light utilization by marine green algal light harvesting complex II at 2.78 Å |
| title_fullStr | Structural insights into blue-green light utilization by marine green algal light harvesting complex II at 2.78 Å |
| title_full_unstemmed | Structural insights into blue-green light utilization by marine green algal light harvesting complex II at 2.78 Å |
| title_short | Structural insights into blue-green light utilization by marine green algal light harvesting complex II at 2.78 Å |
| title_sort | structural insights into blue green light utilization by marine green algal light harvesting complex ii at 2 78 a |
| topic | Codium fragile Cryo-EM Light-harvesting complex Siphonaxanthin–chlorophyll a/b-binding protein (SCP) Intermonomer chlorophyll b macrocluster |
| url | http://www.sciencedirect.com/science/article/pii/S2667160322000242 |
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