ArticleFrontiers in molecular biosciences2026
PHY domain governs structural and photochemical fidelity in the far-red-absorbing state of phytochromes.
Article in Frontiers in molecular biosciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Background: Despite its central role in signaling, the influence of protein architecture on phytochrome structure and reactivity remains poorly understood. Here, we test how removal of the PHY domain reshapes the far-red-absorbing P Methods: We combined femtosecond transient absorption (TA) spectroscopy with solid-state NMR to compare P Results: GAF1-PHY displays a single chromophore conformation with homogeneous photodynamics and a photoconversion quantum yield of 16%. In contrast, GAF1-only exhibits three ground-state subpopulations (NMR) and heterogeneous photodynamics (TA), with kinetically distinct excited-state behaviors and markedly different branching toward Lumi-F photoproduct formation. One subpopulation accounts for ∼95% of photoproduct formation, whereas the other two relax predominantly through nonproductive recovery, yielding an overall photoconversion quantum yield of ∼10%. The productive branch shows a strongly red-shifted stimulated emission consistent with transient deprotonation at ring C or D, and the GAF1-only photoproduct exhibits CBCR-like electronic rearrangements relative to the canonical PHY-stabilized pattern. Conclusion: The PHY domain acts as a structural gatekeeper that suppresses intrinsic chromophore heterogeneity and directs P
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