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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Main Author: Hiroshi Ishikita
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2011-01-01
Series:PLoS ONE
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22039551/?tool=EBI
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spelling 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
collection 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
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