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Ultrafast structural changes within a photosynthetic reaction centre

by Vallejos, Adams , Maj, Michał , Sharma, Amit , Kübel, Joachim , Davidsson, Jan , Groenhof, Gerrit , Hunter, Mark S. , Neutze, Richard , Morozov, Dmitry , Milathianaki, Despina , Robinson, Joseph , Li, Chufeng , Beyerlein, Kenneth R. , Bosman, Robert , Gagnér, Viktor Ahlberg , Dahl, Peter , Carbajo, Sergio , Safari, Cecilia , Liang, Mengning , Johansson, Linda , Westenhoff, Sebastian , Brändén, Gisela , Andersson, Rebecka , Arnlund, David , Katona, Gergely , Dods, Robert , Båth, Petra , Claesson, Elin , Yefanov, Oleksandr , Lisova, Stella , Harimoorthy, Rajiv , Conrad, Chelsie E. , Wickstrand, Cecilia , Williams, Garth J. , Malmerberg, Erik , Hammarin, Greger , Barty, Anton , Berntsen, Peter , Nelson, Garrett , Boutet, Sébastien , DePonte, Daniel P. , Luk, Hoi Ling , Royant, Antoine

in 631/45/535/1266/1265 / 631/57/1464 / Algae / analogs & derivatives / Bacteriochlorophylls / Bacteriochlorophylls - metabolism / Binding Sites / Binding Sites - drug effects / Biochemistry, Molecular Biology / Biofysik / Biophysics / Blastochloris viridis / chemistry / Chlorophyll / Chlorophyll - metabolism / Chlorophyll - radiation effects / Cofactors / Coherent light / Confidence / Crystallography / Cyanobacteria / Cytoplasm / Cytoplasm - metabolism / Diffraction / Diffraction patterns / drug effects / Electron density / Electron Transport / Electron Transport - drug effects / Electrons / enzymology / Humanities and Social Sciences / Hyphomicrobiaceae / Hyphomicrobiaceae - enzymology / Hyphomicrobiaceae - metabolism / Integral membrane proteins / Lasers / Life Sciences / Light / Light sources / metabolism / Methods / Microcrystals / Models, Molecular / Molecular / Molecular Biology / Molekylärbiologi / multidisciplinary / Natural history / Observations / Optical properties / Oxidation-Reduction / Oxidation-Reduction - radiation effects / Pheophytins / Pheophytins - metabolism / Photoexcitation / Photosynthesis / Photosynthetic Reaction Center Complex Proteins / Photosynthetic Reaction Center Complex Proteins - chemistry / Photosynthetic Reaction Center Complex Proteins - metabolism / Photosynthetic Reaction Center Complex Proteins - radiation effects / Photosynthetic reaction centers / Proteins / Protons / radiation effects / Science / Science (multidisciplinary) / Speed / Statistical analysis / Statistical tests / Structural Biology / Structure / Strukturbiologi / Ubiquinone / Ubiquinone - analogs & derivatives / Ubiquinone - metabolism / Vitamin K 2 / Vitamin K 2 - metabolism

2021

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Ultrafast structural changes within a photosynthetic reaction centre

2021

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2021

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Journal Article

Ultrafast structural changes within a photosynthetic reaction centre

Vallejos, Adams,

Maj, Michał,

Sharma, Amit,

Kübel, Joachim,

Davidsson, Jan,

Groenhof, Gerrit,

Hunter, Mark S.,

Neutze, Richard,

Morozov, Dmitry,

Milathianaki, Despina,

Robinson, Joseph,

Li, Chufeng,

Beyerlein, Kenneth R.,

Bosman, Robert,

Gagnér, Viktor Ahlberg,

Dahl, Peter,

Carbajo, Sergio,

Safari, Cecilia,

Liang, Mengning,

Johansson, Linda,

Westenhoff, Sebastian,

Brändén, Gisela,

Andersson, Rebecka,

Arnlund, David,

Katona, Gergely,

Dods, Robert,

Båth, Petra,

Claesson, Elin,

Yefanov, Oleksandr,

Lisova, Stella,

Harimoorthy, Rajiv,

Conrad, Chelsie E.,

Wickstrand, Cecilia,

Williams, Garth J.,

Malmerberg, Erik,

Hammarin, Greger,

Barty, Anton,

Berntsen, Peter,

Nelson, Garrett,

Boutet, Sébastien,

DePonte, Daniel P.,

Luk, Hoi Ling,

Royant, Antoine

2021

Overview

Photosynthetic reaction centres harvest the energy content of sunlight by transporting electrons across an energy-transducing biological membrane. Here we use time-resolved serial femtosecond crystallography 1 using an X-ray free-electron laser 2 to observe light-induced structural changes in the photosynthetic reaction centre of Blastochloris viridis on a timescale of picoseconds. Structural perturbations first occur at the special pair of chlorophyll molecules of the photosynthetic reaction centre that are photo-oxidized by light. Electron transfer to the menaquinone acceptor on the opposite side of the membrane induces a movement of this cofactor together with lower amplitude protein rearrangements. These observations reveal how proteins use conformational dynamics to stabilize the charge-separation steps of electron-transfer reactions. Time-resolved serial femtosecond crystallography is used to reveal the structural changes that stabilize the charge-separation steps of electron-transfer reactions in the photosynthetic reaction centre of Blastochloris viridis on a timescale of picoseconds.

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Publisher

Nature Publishing Group UK,Nature Publishing Group

Subject

631/45/535/1266/1265

/ 631/57/1464

/ Algae

/ analogs & derivatives

/ Bacteriochlorophylls

/ Bacteriochlorophylls - metabolism

/ Binding Sites