ArticleChemistry (Weinheim an der Bergstrasse, Germany)2011
Phototriggering electron flow through Re(I)-modified Pseudomonas aeruginosa azurins.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 51 citations in OpenAlex.
- Electron Transport through a Tryptophan Quadruplex in a Dimeric Azurin Construct.The journal of physical chemistry. B · 2026Article
- Tryptophan to Tryptophan Hole Hopping in an Azurin Construct.The journal of physical chemistry. B · 2024Article
- Photoinduced hole hopping through tryptophans in proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Competing ultrafast photoinduced electron transfer and intersystem crossing of [Re(CO)Theoretical chemistry accounts · 2020Article
- Hole Hopping Across a Protein-Protein Interface.The journal of physical chemistry. B · 2019Article
- Two Tryptophans Are Better Than One in Accelerating Electron Flow through a Protein.ACS central science · 2019Article
- Electron flow through biological molecules: does hole hopping protect proteins from oxidative damage?Quarterly reviews of biophysics · 2015Review
- Solvation-driven charge transfer and localization in metal complexes.Accounts of chemical research · 2015Article
- Tryptophan-to-heme electron transfer in ferrous myoglobins.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Could tyrosine and tryptophan serve multiple roles in biological redox processes?Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2015Article
- Monitoring Long-Range Electron Transfer Pathways in Proteins by Stimulated Attosecond Broadband X-ray Raman Spectroscopy.The journal of physical chemistry letters · 2014Article
- Biochemistry and theory of proton-coupled electron transfer.Chemical reviews · 2014Review
- Tryptophan-accelerated electron flow across a protein-protein interface.Journal of the American Chemical Society · 2013Article
- Hopping Maps for Photosynthetic Reaction Centers().Coordination chemistry reviews · 2013Article
- Electron hopping through proteins.Coordination chemistry reviews · 2012Article
- Charge photoinjection in intercalated and covalently bound [Re(CO)3(dppz)(py)]+-DNA constructs monitored by time-resolved visible and infrared spectroscopy.Journal of the American Chemical Society · 2011Article
- Mass spectrometric characterization of oligomers in Pseudomonas aeruginosa azurin solutions.The journal of physical chemistry. B · 2011Article
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14 authors at 6 institutions in 4 countries.
Funding
Abstract
The [Re(I)(CO)(3)(4,7-dimethyl-1,10-phenanthroline)(histidine-124)(tryptophan-122)] complex, denoted [Re(I)(dmp)(W122)], of Pseudomonas aeruginosa azurin behaves as a single photoactive unit that triggers very fast electron transfer (ET) from a distant (2 nm) Cu(I) center in the protein. Analysis of time-resolved (ps-μs) IR spectroscopic and kinetics data collected on [Re(I)(dmp)(W122)AzM] (in which M=Zn(II), Cu(II), Cu(I); Az=azurin) and position-122 tyrosine (Y), phenylalanine (F), and lysine (K) mutants, together with excited-state DFT/time-dependent (TD)DFT calculations and X-ray structural characterization, reveal the character, energetics, and dynamics of the relevant electronic states of the [Re(I)(dmp)(W122)] unit and a cascade of photoinduced ET and relaxation steps in the corresponding Re-azurins. Optical population of [Re(I)(imidazole-H124)(CO)(3)]→dmp (1)CT states (CT=charge transfer) is followed by around 110 fs intersystem crossing and about 600 ps structural relaxation to a (3)CT state. The IR spectrum indicates a mixed Re(I)(CO)(3),A→dmp/π→π(*)(dmp) character for aromatic amino acids A122 (A=W, Y, F) and Re(I)(CO)(3)→dmp metal-ligand charge transfer (MLCT) for [Re(I)(dmp)(K122)AzCu(II)]. In a few ns, the (3)CT state of [Re(I)(dmp)(W122)AzM] establishes an equilibrium with the [Re(I)(dmp(.-))(W122(.+))AzM] charge-separated state, (3)CS, whereas the (3)CT state of the other Y, F, and K122 proteins decays to the ground state. In addition to this main pathway, (3)CS is populated by fs- and ps-W(indole)→Re(II) ET from (1)CT and the initially "hot" (3)CT states, respectively. The (3)CS state undergoes a tens-of-ns dmp(.-)→W122(.+) ET recombination leading to the ground state or, in the case of the Cu(I) azurin, a competitively fast (≈30 ns over 1.12 nm) Cu(I)→W(.+) ET, to give [Re(I)(dmp(.-))(W122)AzCu(II)]. The overall photoinduced Cu(I)→Re(dmp) ET through [Re(I)(dmp)(W122)AzCu(I)] occurs over a 2 nm distance in <50 ns after excitation, with the intervening fast (3)CT-(3)CS equilibrium being the principal accelerating factor. No reaction was observed for the three Y, F, and K122 analogues. Although the presence of [Re(dmp)(W122)AzCu(II)] oligomers in solution was documented by mass spectrometry and phosphorescence anisotropy, the kinetics data do not indicate any significant interference from the intermolecular ET steps. The ground-state dmp-indole π-π interaction together with well-matched W/W(.+) and excited-state [Re(II)(CO)(3)(dmp(.-))]/[Re(I)(CO)(3)(dmp(.-))] potentials that result in very rapid electron interchange and (3)CT-(3)CS energetic proximity, are the main factors responsible for the unique ET behavior of [Re(I)(dmp)(W122)]-containing azurins.
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