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

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:
Grant/Contract Number:
AC02-06CH11357; SC0002036; DGE-1143954
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
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)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; charge separation; high-throughput mutagenesis; photosynthetic bacteria; rapid screening; time-resolved spectroscopy
OSTI Identifier:
1349060
Alternate Identifier(s):
OSTI ID: 1400564

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., 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.. 2016. "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}
}