Tyrosine deprotonation and associated hydrogen bond rearrangements in a photosynthetic reaction center.
Photosynthetic reaction centers from Blastochloris viridis possess Tyr-L162 located mid-way between the special pair chlorophyll (P) and the heme (heme3). While mutation of the tyrosine does not affect the kinetics of electron transfer from heme3 to P, recent time-resolved Laue diffraction studies r...
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2011
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oai:doaj.org-article:ff06182029344a5797f16fd57f282b302021-11-18T07:35:50ZTyrosine deprotonation and associated hydrogen bond rearrangements in a photosynthetic reaction center.1932-620310.1371/journal.pone.0026808https://doaj.org/article/ff06182029344a5797f16fd57f282b302011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22039551/?tool=EBIhttps://doaj.org/toc/1932-6203Photosynthetic reaction centers from Blastochloris viridis possess Tyr-L162 located mid-way between the special pair chlorophyll (P) and the heme (heme3). While mutation of the tyrosine does not affect the kinetics of electron transfer from heme3 to P, recent time-resolved Laue diffraction studies reported displacement of Tyr-L162 in response to the formation of the photo-oxidized P(+•), implying a possible tyrosine deprotonation event. pK(a) values for Tyr-L162 were calculated using the corresponding crystal structures. Movement of deprotonated Tyr-L162 toward Thr-M185 was observed in P(+•) formation. It was associated with rearrangement of the H-bond network that proceeds to P via Thr-M185 and His-L168.Hiroshi IshikitaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 10, p e26808 (2011) |
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Medicine R Science Q Hiroshi Ishikita Tyrosine deprotonation and associated hydrogen bond rearrangements in a photosynthetic reaction center. |
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Photosynthetic reaction centers from Blastochloris viridis possess Tyr-L162 located mid-way between the special pair chlorophyll (P) and the heme (heme3). While mutation of the tyrosine does not affect the kinetics of electron transfer from heme3 to P, recent time-resolved Laue diffraction studies reported displacement of Tyr-L162 in response to the formation of the photo-oxidized P(+•), implying a possible tyrosine deprotonation event. pK(a) values for Tyr-L162 were calculated using the corresponding crystal structures. Movement of deprotonated Tyr-L162 toward Thr-M185 was observed in P(+•) formation. It was associated with rearrangement of the H-bond network that proceeds to P via Thr-M185 and His-L168. |
format |
article |
author |
Hiroshi Ishikita |
author_facet |
Hiroshi Ishikita |
author_sort |
Hiroshi Ishikita |
title |
Tyrosine deprotonation and associated hydrogen bond rearrangements in a photosynthetic reaction center. |
title_short |
Tyrosine deprotonation and associated hydrogen bond rearrangements in a photosynthetic reaction center. |
title_full |
Tyrosine deprotonation and associated hydrogen bond rearrangements in a photosynthetic reaction center. |
title_fullStr |
Tyrosine deprotonation and associated hydrogen bond rearrangements in a photosynthetic reaction center. |
title_full_unstemmed |
Tyrosine deprotonation and associated hydrogen bond rearrangements in a photosynthetic reaction center. |
title_sort |
tyrosine deprotonation and associated hydrogen bond rearrangements in a photosynthetic reaction center. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2011 |
url |
https://doaj.org/article/ff06182029344a5797f16fd57f282b30 |
work_keys_str_mv |
AT hiroshiishikita tyrosinedeprotonationandassociatedhydrogenbondrearrangementsinaphotosyntheticreactioncenter |
_version_ |
1718423263529402368 |