Time-resolved electron paramagnetic resonance (TR-EPR), combined with magnetophotoselection (MPS), provides a powerful approach to probe exciton states in multichromophoric systems where photoexcitation populates a triplet state localized on a specific chromophore. This scenario occurs in the peridinin–chlorophyll protein (PCP) from dinoflagellates, which contains clusters of peridinins surrounding chlorophyll a. Here, we present MPS-TR-EPR data for PCP from Heterocapsa pygmaea and a high-salt PCP variant from Amphidinium carterae. Spectral analysis reveals the orientation of the optical transition dipole moments (TDMs), reflecting the chromophore contributions to the exciton states. The results indicate a predominant role of Per614/624 in the lowest singlet exciton state, consistent with theoretical models, while, at the same time, also suggesting refinements to better align the models with the experimentally determined TDM orientations. These findings provide constraints relevant to understanding molecular strategies for optimizing light absorption and energy transfer in light-harvesting complexes.

We have created modified protein variants by introducing a non-canonical amino acid p-azido-L-phenylalanine (azF) into defined positions for photochemically-induced covalent attachment to graphene. Attachment of GFP, TEM and cyt b562 proteins was verified through a combination of atomic force and scanning tunnelling microscopy, resistance measurements, Raman data and fluorescence measurements. This method can in principle be extended to any protein which can be engineered in this way without adversely affecting its structural stability.

Post-translational modification (PTM) modulates and supplements protein functionality. In nature this high precision event requires specific motifs and/or associated modification machinery. To overcome the inherent complexity that hinders PTM's wider use, we have utilized a non-native biocompatible Click chemistry approach to site-specifically modify TEM b-lactamase that adds new functionality. In silico modelling was used to design TEM b-lactamase variants with the non-natural amino acid p-azido-Lphenylalanine (azF) placed at functionally strategic positions permitting residue-specific modification with alkyne adducts by exploiting strain-promoted azide–alkyne cycloaddition. Three designs were implemented so that the modification would: (i) inhibit TEM activity (Y105azF); (ii) restore activity compromised by the initial mutation (P174azF); (iii) facilitate assembly on pristine graphene (W165azF). A dibenzylcyclooctyne (DBCO) with amine functionality was enough to modulate enzymatic activity. Modification of TEMW165azF with a DBCO–pyrene adduct had little effect on activity despite the modification site being close to a key catalytic residue but allowed directed assembly of the enzyme on graphene, potentially facilitating the construction of protein-gated carbon transistor systems.