Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 185-192 |
| Number of pages | 8 |
| Journal | Journal of the American Chemical Society |
| Volume | 140 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Jan 10 2018 |
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ASJC Scopus subject areas
- Catalysis
- Chemistry(all)
- Biochemistry
- Colloid and Surface Chemistry
Cite this
Pourbaix Diagram, Proton-Coupled Electron Transfer, and Decay Kinetics of a Protein Tryptophan Radical : Comparing the Redox Properties of W32 • and Y32 • Generated Inside the Structurally Characterized α3W and α3Y Proteins. / Glover, Starla D.; Tyburski, Robin; Liang, Li; Tommos, Cecilia; Hammarström, Leif.
In: Journal of the American Chemical Society, Vol. 140, No. 1, 10.01.2018, p. 185-192.Research output: Contribution to journal › Article
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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
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 -