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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doaj-ff06182029344a5797f16fd57f282b302021-03-04T01:26:20ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-01610e2680810.1371/journal.pone.0026808Tyrosine deprotonation and associated hydrogen bond rearrangements in a photosynthetic reaction center.Hiroshi IshikitaPhotosynthetic 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.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22039551/?tool=EBI |
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DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Hiroshi Ishikita |
spellingShingle |
Hiroshi Ishikita Tyrosine deprotonation and associated hydrogen bond rearrangements in a photosynthetic reaction center. PLoS ONE |
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) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2011-01-01 |
description |
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. |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22039551/?tool=EBI |
work_keys_str_mv |
AT hiroshiishikita tyrosinedeprotonationandassociatedhydrogenbondrearrangementsinaphotosyntheticreactioncenter |
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