High Yield of B-Side Electron Transfer at 77 K in the Photosynthetic Reaction Center Protein from Rhodobacter sphaeroides

Magdaong, Nikki Cecil M.; Faries, Kaitlyn M.; Buhrmaster, James C.; Tira, Gregory A.; Wyllie, Ryan M.; Kohout, Claire E.; Hanson, Deborah K.; Laible, Philip D.; Holten, Dewey; Kirmaier, Christine

doi:10.1021/acs.jpcb.2c05905

Title: High Yield of B-Side Electron Transfer at 77 K in the Photosynthetic Reaction Center Protein from Rhodobacter sphaeroides

Journal Article · Mon Oct 31 00:00:00 EDT 2022 · Journal of Physical Chemistry. B

DOI:https://doi.org/10.1021/acs.jpcb.2c05905· OSTI ID:1905538

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^[2]; Tira, Gregory A. ^[2]; Wyllie, Ryan M. ^[2]; Kohout, Claire E. ^[2];

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Washington Univ., St. Louis, MO (United States)
Argonne National Lab. (ANL), Argonne, IL (United States)

In this work, the primary electron transfer (ET) processes at 295 K and 77 K are compared for the Rhodobacter sphaeroides reaction center (RC) pigment-protein complex from thirteen mutants including a wild-type control. The engineered RCs bear mutations in the L and M polypeptides that largely inhibit ET from the excited state P* of the primary electron donor (P, a bacteriochlorophyll dimer) to the normally photoactive A-side cofactors and enhance ET to the C₂-symmetry related, and normally photoinactive, B-side cofactors. P* decay is multi-exponential at both temperatures and modeled as arising from subpopulations that differ in contributions of two-step ET (e.g., P* → P⁺B_B^– → P⁺H_B^–), one-step superexchange ET (e.g., P* → P⁺H_B^–) and P* → ground state. [H_B and B_B are monomeric bacteriopheophytin and bacteriochlorophyll, respectively.] The relative abundances of the subpopulations and the inherent rate constants of the P* decay routes vary with temperature. Regardless, ET to produce P⁺H_B^– is generally faster at 77 K than at 295 K by about a factor of two. A key finding is that the yield of P⁺H_B^–, which ranges from ~5% to ~90% among the mutant RCs, is essentially the same at 77 K as at 295 K in each case. Overall, the results show that ET from P* to the B-side cofactors in these mutants does not require thermal activation and involves combinations of ET mechanisms analogous to those operative on the A side in the native RC.

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Research Organization:: Washington Univ., St. Louis, MO (United States); Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: SC0002036; AC02-06CH11357

OSTI ID:: 1905538

Alternate ID(s):: OSTI ID: 1991599

Journal Information:: Journal of Physical Chemistry. B, Vol. 126, Issue 44; ISSN 1520-6106

Publisher:: American Chemical SocietyCopyright Statement

Country of Publication:: United States

Language:: English

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