TY - JOUR
T1 - Pourbaix Diagram, Proton-Coupled Electron Transfer, and Decay Kinetics of a Protein Tryptophan Radical
T2 - Comparing the Redox Properties of W32• and Y32• Generated Inside the Structurally Characterized α3W and α3Y Proteins
AU - Glover, Starla D.
AU - Tyburski, Robin
AU - Liang, Li
AU - Tommos, Cecilia
AU - Hammarström, Leif
N1 - Funding Information:
Funding was provided by the National Institutes of Health Grant GM079190 (C.T.) and the Swedish Research Council Grants 621-2012-3926 and 2016-04271 (L.H.). Valuable discussions with Professor Josh Wand are gratefully acknowledged.
PY - 2018/1/10
Y1 - 2018/1/10
N2 - Protein-based "hole" hopping typically involves spatially arranged redox-active tryptophan or tyrosine residues. Thermodynamic information is scarce for this type of process. The well-structured α3W model protein was studied by protein film square wave voltammetry and transient absorption spectroscopy to obtain a comprehensive thermodynamic and kinetic description of a buried tryptophan residue. A Pourbaix diagram, correlating thermodynamic potentials (E°′) with pH, is reported for W32 in α3W and compared to equivalent data recently presented for Y32 in α3Y (Ravichandran, K. R.; Zong, A. B.; Taguchi, A. T.; Nocera, D. G.; Stubbe, J.; Tommos, C. J. Am. Chem. Soc. 2017, 139, 2994-3004). The α3W Pourbaix diagram displays a pKOX of 3.4, a E°′(W32(N•+/NH)) of 1293 mV, and a E°′(W32(N•/NH); pH 7.0) of 1095 ± 4 mV versus the normal hydrogen electrode. W32(N•/NH) is 109 ± 4 mV more oxidizing than Y32(O•/OH) at pH 5.4-10. In the voltammetry measurements, W32 oxidation-reduction occurs on a time scale of about 4 ms and is coupled to the release and subsequent uptake of one full proton to and from bulk. Kinetic analysis further shows that W32 oxidation likely involves pre-equilibrium electron transfer followed by proton transfer to a water or small water cluster as the primary acceptor. A well-resolved absorption spectrum of W32• is presented, and analysis of decay kinetics show that W32• persists ∼104 times longer than aqueous W• due to significant stabilization by the protein. The redox characteristics of W32 and Y32 are discussed relative to global and local protein properties.
AB - Protein-based "hole" hopping typically involves spatially arranged redox-active tryptophan or tyrosine residues. Thermodynamic information is scarce for this type of process. The well-structured α3W model protein was studied by protein film square wave voltammetry and transient absorption spectroscopy to obtain a comprehensive thermodynamic and kinetic description of a buried tryptophan residue. A Pourbaix diagram, correlating thermodynamic potentials (E°′) with pH, is reported for W32 in α3W and compared to equivalent data recently presented for Y32 in α3Y (Ravichandran, K. R.; Zong, A. B.; Taguchi, A. T.; Nocera, D. G.; Stubbe, J.; Tommos, C. J. Am. Chem. Soc. 2017, 139, 2994-3004). The α3W Pourbaix diagram displays a pKOX of 3.4, a E°′(W32(N•+/NH)) of 1293 mV, and a E°′(W32(N•/NH); pH 7.0) of 1095 ± 4 mV versus the normal hydrogen electrode. W32(N•/NH) is 109 ± 4 mV more oxidizing than Y32(O•/OH) at pH 5.4-10. In the voltammetry measurements, W32 oxidation-reduction occurs on a time scale of about 4 ms and is coupled to the release and subsequent uptake of one full proton to and from bulk. Kinetic analysis further shows that W32 oxidation likely involves pre-equilibrium electron transfer followed by proton transfer to a water or small water cluster as the primary acceptor. A well-resolved absorption spectrum of W32• is presented, and analysis of decay kinetics show that W32• persists ∼104 times longer than aqueous W• due to significant stabilization by the protein. The redox characteristics of W32 and Y32 are discussed relative to global and local protein properties.
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U2 - 10.1021/jacs.7b08032
DO - 10.1021/jacs.7b08032
M3 - Article
C2 - 29190082
AN - SCOPUS:85038596929
VL - 140
SP - 185
EP - 192
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 1
ER -