Protein surface interactions probed by magnetic field effects on chemical reactions.
Here we have employed the effects of weak static magnetic fields (not exceeding 46 mT) on radical recombination reactions to investigate protein-substrate interactions. Pulsed laser excitation of an aqueous solution of anthraquinone-2,6-disulfonate (AQDS(2-)) and either hen egg white lysozyme (HEWL) or bovine serum albumin (BSA) produces the triplet state of the radical pair (T)[AQDS(3-*) Trp(*)] by a photoinduced electron transfer reaction from tryptophan residues. Time-resolved absorption techniques were employed to study the recombination characteristics of these radical pairs at different static magnetic fields and ionic strengths. The experimental data in connection with the simulated curves unequivocally show that the radical pair has a lifetime of the order of microseconds in both systems (HEWL and BSA). However, the radical pair is embedded within a binding pocket of the BSA protein, while the (otherwise identical) radical pair, being subject to attractive Coulomb forces, resides on the protein surface in the HEWL system.
Maeda
Kiminori
K
Centre for Advanced Electron Spin Resonance, Department of Chemistry, University of Oxford, Oxford OX1 3TA, UK. kiminori.maeda@chem.ox.ac.uk
Robinson
Alexander J
AJ
Henbest
Kevin B
KB
Dell
Emma J
EJ
Timmel
Christiane R
CR
D000818:Animals; D000880:Anthraquinones / Q000737:chemistry; D002417:Cattle; D002645:Chickens; D004579:Electron Transport; D008280:Magnetics; D008958:Models, Molecular; D009113:Muramidase / Q000032:analysis*; D010782:Photolysis; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000032:analysis*; D014364:Tryptophan / Q000737:chemistry
D000880:Anthraquinones; C408124:anthraquinone-2,6-disulfonate; D012710:Serum Albumin, Bovine; D014364:Tryptophan; C421864:hen egg lysozyme; D009113:Muramidase