To improve the power conversion efficiency of solar cells, it is important to understand the underlying relaxation mechanisms of photogenerated charge carriers in organic semiconductors. In this work, we studied the charge carrier dynamics of diketopyrrolopyrrole-linked tetrabenzoporphyrin thin films where the diketopyrrolopyrrole unit has two n-butyl groups, abbreviated as C4-DPP-BP. We used time-resolved terahertz (THz) spectroscopy to track charge carrier dynamics with excitations at 800 and 400 nm. Compared with tetrabenzoporphyrin (BP), the extension of π-electron delocalization to the diketopyrrolopyrrole peripherals leads to an increase in absorption in the near-infrared region. Following the excitation at 800 nm, we found that the transient THz signals in C4-DPP-BP thin films decay with time constants of 0.5 and 9.1 ps, with small residual components. With excitation at 400 nm, we found that the transient THz signals decay with time constants of 0.4 and 7.5 ps. On the basis of the similarity of the decay profiles of the transient THz signals obtained with excitations at 400 and 800 nm, we considered that the decaying components are due to charge carrier recombination and/or trapping at defect sites, which do not depend on the excess energy of the photoexcitation. In contrast to BP, even without an electron acceptor, we observed the finite offset of the transient THz signals at 100 ps, demonstrating the existence of long-lived charge carriers. We also measured the photoconductivity spectra of C4-DPP-BP thin films with the excitation at both 800 and 400 nm. It was found that the spectra can be fitted by the Drude-Smith model. From these results, it was determined that the charge carriers are localized right after photoexcitation. At 0.4 ps, the product of the quantum yield of charge generation and mobility of charge carriers at 400 nm is approximately twice that obtained at 800 nm. We discuss the implications of the excess excitation energy in organic semiconductor-based devices.

Blue light sensor using flavin (BLUF) proteins consist of flavin-binding BLUF domains and functional domains. Upon blue light excitation, the hydrogen bond network around the flavin chromophore changes, and the absorption spectrum in the visible region exhibits a red shift. Ultimately, the light information received in the BLUF domain is transmitted to the functional region. It has been believed that this red shift is complete within nanoseconds. In this study, slow reaction kinetics were discovered in milliseconds (τ1- and τ2-phase) for all the BLUF proteins examined (AppA, OaPAC, BlrP1, YcgF, PapB, SyPixD, and TePixD). Despite extensive reports on BLUF, this is the first clear observation of the BLUF protein absorption change with the duration in the millisecond time region. From the measurements of some domain-deleted mutants of OaPAC and two chimeric mutants of PixD proteins, it was found that the slower dynamics (τ2-phase) are strongly affected by the size and nature of the C-terminal region adjacent to the BLUF domain. Hence, this millisecond reaction is a significant indicator of conformational changes in the C-terminal region, which is essential for the biological functions. On the other hand, the τ1-phase commonly exists in all BLUF proteins, including any mutants. The origin of the slow dynamics was studied using site-specific mutants. These results clearly show the importance of Trp in the BLUF domain. Based on this, a reaction scheme for the BLUF reaction is proposed.

Two asymmetric double quantum wells of different coupling strengths (barrier widths) were grown via molecular beam epitaxy, both samples allowing tunneling. Photoluminescence was measured at 10 and 300 K to provide evidence of tunneling, barrier dependence, and structural uniformity. Carrier dynamics at room temperature was investigated by optical pump terahertz probe (OPTP) spectroscopy. Carrier population decay rates were obtained and photoconductivity spectra were analyzed using the Drude model. This work demonstrates that carrier, and possibly tunneling dynamics in asymmetric double quantum well structures may be studied at room temperature through OPTP spectroscopy.

BLUF (blue light sensor using flavin) proteins consist of flavin-binding BLUF domains and functional domains. Upon blue light excitation, the hydrogen bond network around the flavin chromophore changes, and the absorption spectrum in the visible region exhibits red-shift. Ultimately, the light information received in the BLUF domain is transmitted to the functional region. It has been believed that this red-shift is complete within nanoseconds. Contrary to this commonly accepted scheme, in this study, slow reaction kinetics were discovered in milliseconds (τ1- and τ2-phase) for all the BLUF proteins examined (AppA, OaPAC, BlrP1, YcgF, PapB, SyPixD, and TePixD). Despite extensive reports on BLUF, this is the first clear observation of the BLUF protein absorption change with the duration in the millisecond time region. From the measurements of some domain-deleted mutants of OaPAC and two chimeric mutants of PixD proteins, it was found that the slower dynamics (τ2-phase) are strongly affected by the size and nature of the C-terminal region adjacent to the BLUF domain. Hence, this millisecond reaction is a significant indicator of conformational changes in the C-terminal region, which is essential for the biological functions. On the other hand, the τ1-phase commonly exists in all BLUF proteins, including any mutants. The origin of the slow dynamics was studied using site-specific mutants. These results clearly show the importance of Trp in the BLUF domain. Based on this, a reaction scheme for the BLUF reaction is proposed.

A sensor of blue-light using flavin adenine dinucleotide (BLUF) is a typical blue light photoreceptor domain that is found in many photosensor proteins in bacteria and some eukaryotic algae. SyPixD in Synechocystis is one of the well-studied BLUF proteins. In the dark state, it forms a decamer and, upon photoexcitation, a dissociation reaction takes place to yield dimers. Such change in the intermolecular interactions of the protomers is important for the biological function. The effect of the N-and C-terminal sequences on the stability of SyPixD oligomeric states and photoreactions of SyPixD were studied to understand how the oligomeric form is maintained with weak interaction. It was found that a few residues that frequently persist at the Nterminus after removing a tag for purification are sensitive to the stability of the decamer structure. Even two or three residues at the N-terminus considerably reduces decamer stability, whereas four or more residues completely prevent decamer formation. Unexpectedly, truncating C-terminal sequences, which locate far from any protomer interface and of which structure is undetermined in crystal structure, also destabilizes the decamer structure. This destabilization is also apparent from the dissociation reaction dynamics detected by the transient grating and transient absorption measurements.The dissociation reaction is faster and the yield increases when the C-terminus does not contain seven amino acid residues. Photoexcitation induces a conformational change in the C-terminus of the decamer but not the dimer.