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Title: Species differences in unlocking B-side electron transfer in bacterial reaction centers

Abstract

The structure of the bacterial photosynthetic reaction center (RC) reveals symmetry-related electron transfer (ET) pathways, but only one path is used in native RCs. Analogous mutations have been made in two Rhodobacter (R.) species. A glutamic acid at position 133 in the M subunit increases transmembrane charge separation via the naturally inactive (B-side) path through impacts on primary ET in mutant R. sphaeroidesRCs. Prior work showed that the analogous substitution in the R. capsulatusRC also increases B-side activity, but mainly affects secondary ET. Finally, the overall yields of transmembrane ET are similar, but enabled in fundamentally different ways.

Authors:
 [1];  [2];  [1];  [1];  [1];  [2];  [2];  [1]
  1. Argonne National Lab. (ANL), Argonne, IL (United States). Biosciences Division
  2. Washington Univ., St. Louis, MO (United States). Dept. of Chemistry
Publication Date:
Research Org.:
Washington Univ., St. Louis, MO (United States); Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22); USDOE Office of Science (SC), Workforce Development for Teachers and Scientists (WDTS) (SC-27); National Science Foundation (NSF)
OSTI Identifier:
1349060
Alternate Identifier(s):
OSTI ID: 1400564
Grant/Contract Number:  
AC02-06CH11357; SC0002036; DGE-1143954
Resource Type:
Accepted Manuscript
Journal Name:
FEBS Letters
Additional Journal Information:
Journal Volume: 590; Journal Issue: 16; Journal ID: ISSN 0014-5793
Publisher:
Federation of European Biochemical Societies
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; charge separation; high-throughput mutagenesis; photosynthetic bacteria; rapid screening; time-resolved spectroscopy

Citation Formats

Dylla, Nicholas P., Faries, Kaitlyn M., Wyllie, Ryan M., Swenson, Angela M., Hanson, Deborah K., Holten, Dewey, Kirmaier, Christine, and Laible, Philip D. Species differences in unlocking B-side electron transfer in bacterial reaction centers. United States: N. p., 2016. Web. doi:10.1002/1873-3468.12264.
Dylla, Nicholas P., Faries, Kaitlyn M., Wyllie, Ryan M., Swenson, Angela M., Hanson, Deborah K., Holten, Dewey, Kirmaier, Christine, & Laible, Philip D. Species differences in unlocking B-side electron transfer in bacterial reaction centers. United States. doi:10.1002/1873-3468.12264.
Dylla, Nicholas P., Faries, Kaitlyn M., Wyllie, Ryan M., Swenson, Angela M., Hanson, Deborah K., Holten, Dewey, Kirmaier, Christine, and Laible, Philip D. Tue . "Species differences in unlocking B-side electron transfer in bacterial reaction centers". United States. doi:10.1002/1873-3468.12264. https://www.osti.gov/servlets/purl/1349060.
@article{osti_1349060,
title = {Species differences in unlocking B-side electron transfer in bacterial reaction centers},
author = {Dylla, Nicholas P. and Faries, Kaitlyn M. and Wyllie, Ryan M. and Swenson, Angela M. and Hanson, Deborah K. and Holten, Dewey and Kirmaier, Christine and Laible, Philip D.},
abstractNote = {The structure of the bacterial photosynthetic reaction center (RC) reveals symmetry-related electron transfer (ET) pathways, but only one path is used in native RCs. Analogous mutations have been made in two Rhodobacter (R.) species. A glutamic acid at position 133 in the M subunit increases transmembrane charge separation via the naturally inactive (B-side) path through impacts on primary ET in mutant R. sphaeroidesRCs. Prior work showed that the analogous substitution in the R. capsulatusRC also increases B-side activity, but mainly affects secondary ET. Finally, the overall yields of transmembrane ET are similar, but enabled in fundamentally different ways.},
doi = {10.1002/1873-3468.12264},
journal = {FEBS Letters},
number = 16,
volume = 590,
place = {United States},
year = {2016},
month = {6}
}

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Cited by: 1 work
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