New Insights into the Reaction Paths of 4‑Carboxybenzophenone Triplet with Oligopeptides Containing N- and C‑Terminal Methionine Residues

• Published in: The journal of physical chemistry. B 2017-05, Vol.121 (20), p.5247-5258
• Main Authors: Filipiak, Piotr, Bobrowski, Krzysztof, Hug, Gordon L, Pogocki, Dariusz, Schöneich, Christian, Marciniak, Bronislaw
• Format: Article
• Language: English
• Subjects: Benzophenones - chemistry; Methionine - chemistry; Oligopeptides - chemistry; Quantum Theory
• ISSN: 1520-6106; 1520-5207
• DOI: 10.1021/acs.jpcb.7b01119

The oxidation processes of l-Met-(Pro) n -l-Met peptides that contain two Met residues located on the N and C termini and separated by a defined number (n = 0–4) of proline residues were investigated in aqueous solutions using laser flash photolysis. The use of such peptides allowed for distance control between the sulfur atoms located in the side chains of the Met residues. Interactions between side chains of the Met residues were probed by the observation of transients with σ*-type 2c-3e (S∴S)+, (S∴N)+, and (S∴O)+ bonds as well as of α-(alkylthio)­alkyl radicals (αS). This approach enabled the monitoring, in real time, of the efficiency and kinetics of interactions between amino acid chains. Such knowledge is important, inter alia, for long-distance electron-transfer (ET) processes because amino acid side chains can serve as relay stations. The yields of these transients (measured as quantum yields (Φ)) were found to be dependent on the number of Pro residues, however, not dependent in a simple way on the average distance between sulfur atoms in Met residues. A decrease in the yield of the (S∴S)+ species with the number of Pro residues occurred at the expense of an increase in the yields of intramolecular three electron-bonded (S∴O)+/(S∴N)+ radical cations and αS radicals. These observations were rationalized by the fact that the time required for adequate overlap of the bonding orbitals is a key factor effecting the yield of the (S∴S)+ species. The time, however, can be controlled not only by the average distance but also by the specific geometrical and conformational properties of the peptide molecules.