PICOSECOND LASER PHOTOLYSIS STUDIES OF FLUORESCENCE QUENCHING MECHANISMS OF FLAVIN: A DIRECT OBSERVATION OF INDOLE‐FLAVIN SINGLET CHARGE TRANSFER STATE FORMATION IN SOLUTIONS and FLAVOENZYMES

Karen, Akiya; Ikeda, Noriaki; Mataga, Noboru; Tanaka, Fumio

doi:10.1111/j.1751-1097.1983.tb04507.x

Cited by 61 publications

(63 citation statements)

References 18 publications

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“…In these flavoproteins, aromatic amino acids such as tryptophan (Trp) or tyrosine (Tyr) are located near the isoalloxazine ring (Iso) of flavins. It was found by means of picosecond [19,20] and femtosecond-resolved [21] transient absorption spectroscopy that ET processes from Trp or Tyr to the excited Iso in flavoproteins were responsible for the quenching. Fluorescence decays of several flavoproteins, which were believed to be non-fluorescent, were observed in the time domain of femtoseconds/picoseconds by a fluorescence up-conversion technique [22][23][24][25][26][27].…”

Section: Introductionmentioning

confidence: 99%

Analyses of donor–acceptor distance-dependent rates of photo-induced electron transfer in flavoproteins with three kinds of electron transfer theories

et al. 2008

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Section: Introductionmentioning

confidence: 99%

Analyses of donor–acceptor distance-dependent rates of photo-induced electron transfer in flavoproteins with three kinds of electron transfer theories

et al. 2008

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“…E-mail: mztn@chem.sci.osaka-u.ac.jp in a protein, ET from the aromatic amino acid residues can take place, thus quenching the flavin fluorescence. It was demonstrated by transient absorption spectroscopy that the quenching process of flavin fluorescence can be ascribed to a photoinduced ET from the Trp or Tyr to the excited isoalloxazine of flavins in solution 5 and in flavoproteins. 6 The photochemistry of various flavoproteins has also been investigated by means of a fluorescence upconversion method.…”

Section: Introductionmentioning

confidence: 99%

Photoinduced electron transfer in glucose oxidase: a picosecond time‐resolved ultraviolet resonance Raman study

Fujiwara

Mizutani

2008

J Raman Spectroscopy

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Picosecond time-resolved ultraviolet resonance Raman (UVRR) spectroscopy has been applied to photoinduced electron transfer (ET) of glucose oxidase (GOD). In this study, we succeeded in directly observing changes in the aromatic amino acid residues in the photoinduced ET of GOD for the first time. UVRR spectra excited at 226 nm showed bands from Trp and Tyr residues. An intensity decrease of the Trp UVRR bands and the appearance of the UVRR bands attributable to Trp ·+ were observed in the time-resolved spectra. In the time-resolved UVRR spectra excited at 240 nm, the intensity decrease of the flavin adenine dinucleotide (FAD) bands was also observed on the same time scale. These results showed that the Trp residue(s) serves as an electron donor to excited-state FAD in the photoinduced ET of GOD. The comparison of the temporal changes of the Trp and FAD band intensities suggested that the ET from the Trp residue(s) to the FAD occurs with a time constant of ∼1.5 ps.

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“…For example, it has been known for many decades that flavinoid compounds such as flavin and riboflavin will bind to betacarbolines and other indoles such as serotonin to form charge-transfer complexes [81][82][83]. The chemistry of these complexes has been very well-characterized [84][85][86][87] and has been implicated in the specificity of flavin binding to the indole tryptophan within flavoprotein enzymes such as flavin monooxygenase, N-methyl-tryptophan oxidase, and cytochrome P450 [88,89]. Thus, the simple complexation reaction found in solution appears to have been adapted to complex protein binding sites by evolution, so that studying one yields clues about the other.…”

Section: Aromatic Compound Complexes Involving Vi-taminsmentioning

confidence: 99%

Small Molecule Complementarity As A Source of Novel Pharmaceutical Agents and Combination Therapies

Root‐Bernstein¹,

Dillon²

2008

CPD

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Many examples of specific binding between small molecules are known that are associated with modified physiological and pharmacological activities. Conversely, the antagonism or synergism of small molecules is often correlated with specific binding between the molecules. It follows that small molecule binding can be used as a relatively quick, easy, and specific screen for functionally useful drug actions and interactions. These actions and interactions may manifest themselves as functional antagonisms; binding may correlate with enhancement or synergism; the formation of some complexes may yield clues about how drugs may be targeted to specific cell types in vivo and provide leads for the development of antidotes for drug overdoses or poisoning; the binding of one molecule to another may mimic receptor binding; and complexation may provide novel ways of protecting and delivering drugs. Relevant examples from each type of application are reviewed involving peptide-peptide interactions; peptide-aromatic compound interactions; aromatic-aromatic compound interactions; vitamin-aromatic compound interactions; and polycyclic compound interactions. We argue that screening for molecular complementarity of small molecules turns ligands such as neurotransmitters and their metabolites, hormones, and drugs themselves, into direct targets of drug development that can augment screening new compounds for activity against receptors and second messenger systems. We believe that the small molecule complementarity approach is novel, fruitful and under-utilized.

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PICOSECOND LASER PHOTOLYSIS STUDIES OF FLUORESCENCE QUENCHING MECHANISMS OF FLAVIN: A DIRECT OBSERVATION OF INDOLE‐FLAVIN SINGLET CHARGE TRANSFER STATE FORMATION IN SOLUTIONS and FLAVOENZYMES

Cited by 61 publications

References 18 publications

Analyses of donor–acceptor distance-dependent rates of photo-induced electron transfer in flavoproteins with three kinds of electron transfer theories

Analyses of donor–acceptor distance-dependent rates of photo-induced electron transfer in flavoproteins with three kinds of electron transfer theories

Photoinduced electron transfer in glucose oxidase: a picosecond time‐resolved ultraviolet resonance Raman study

Small Molecule Complementarity As A Source of Novel Pharmaceutical Agents and Combination Therapies

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