Nonpigmented PsbR is involved in the integrity of excitation landscape in higher plant photosystem II, a case study in Arabidopsis thaliana and a mutant
Journal Article
·
· Photosynthesis Research
- Washington University in St. Louis, MO (United States)
- Saint Louis University, MO (United States); IPS Academy, Indore (India)
- Washington University in St. Louis, MO (United States); University of Wisconsin-Madison, WI (United States)
- Saint Louis University, MO (United States)
PsbR is a nonpigmented 10 kDa protein in Photosystem II (PSII) in algae and plants. A recent structural study clarified its enigmatic structural location in a Photosystem II megacomplex that has baffled the community for more than four decades. Our current study interrogates whether absence of PsbR affects the overall dynamics of excitation energy migration within light harvesting complexes (LHC) and PSII super assemblies using highly-active PSII membrane particles, so-called BBY particles, isolated from a PsbR deletion mutant (ΔPsbR) of Arabidopsis thaliana. A femto-second (fs)-time-resolved transient absorption experimentation recorded at 77 K with selective excitation of Chl b which is exclusively present in LHCs enabled us to resolve the temporal differences in LHC→LHC and LHC→PSII excitation energy transfer steps. By applying specific target spectro-kinetic models to the transient absorption datasets, we demonstrated that the time constants of Chl aLHC → Chl aLHC excitation transfer significantly elongates in the ΔPsbR LHC-PSII particles, suggestive of the decreased aggregation level of photosynthetic proteins in the mutant. These findings highlight excitation energy transfer integrity in LHC-PSII assembly is not only determined by the pigmented light-harvesting complexes, but also synergistically by the nonpigmented PSII components. Furthermore, the disturbed integrity in dynamics of excitation energy transfer pathway within LHC-PSII supercomplex is discussed in the context of the altered LHC-PSII megacomplexes type I and II architectures which result from the absence of the PsbR protein in higher plant PSII.
- Research Organization:
- Saint Louis University, MO (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- Grant/Contract Number:
- SC0025019
- OSTI ID:
- 3000718
- Journal Information:
- Photosynthesis Research, Journal Name: Photosynthesis Research Journal Issue: 3 Vol. 163; ISSN 0166-8595; ISSN 1573-5079
- Publisher:
- Springer Science and Business Media LLCCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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