Primary Processes in the Photochemistry of Proteins

Grossweiner, Leonard I.; Blum, Amy Szuchmacher; Brendzel, Avrom M.

doi:10.1007/978-1-4615-9203-7_7

Cited by 14 publications

(4 citation statements)

References 30 publications

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“…⑀ M ϳ 1000 M Ϫ1 cm Ϫ1 for thymine) (64). Furthermore, quantum yields for UVB inactivation of UVB-sensitive aminoacids (⌽ IN ) in proteins show values similar to those for the induction of CPD in DNA, which might lead to inhibition of gene expression and/or replication (65). At a wavelength of 280 nm, Grossweiner reported values for ⌽ IN in the range of 0.3 to 2%, depending of the proteins investigated (66).…”

Section: Dose Dependence Of Repair Time Constantmentioning

confidence: 89%

The Dose Dependence of Cyclobutane Dimer Induction and Repair in UVB-irradiated Human Keratinocytes¶

Greinert

Boguhn

Harder

et al. 2000

Photochem Photobiol

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UVB and UVA components of the solar spectrum or from artificial UV-sources might be important etiological factors for the induction and development of skin cancer. In particular, deficiencies in the capacity to repair UV-induced DNA-lesions have been linked to this phenomenon. However, until now only limited data are available on the biological and physical parameters governing repair capacity. We have, therefore, developed a flowcytometric assay using fluorescence-labeled monoclonal antibodies to study the dose-dependence of induction and repair of UVB-induced cyclobutane pyrimidine dimers in a spontaneously immortalized keratinocytic cell line (HaCaT). Our results show that the kinetics of recognition and incision of UVB-induced DNA lesions slows down by a factor of about 3 in a dose range of 100-800 J m-2. Furthermore, a thorough analysis of repair kinetics indicates that this reduction in repair capacity might not be dependent on saturation of enzymatic repair capacity (Michaelis-Menten) but may be caused by a UV-induced impairment of enzymes involved in DNA repair. Because this effect is evident in vitro at doses comparable to the minimal erythemal dose in vivo, our results might have significant impact on risk assessment for UV-induced carcinogenesis.

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Section: Dose Dependence Of Repair Time Constantmentioning

confidence: 89%

The Dose Dependence of Cyclobutane Dimer Induction and Repair in UVB-irradiated Human Keratinocytes¶

Greinert

Boguhn

Harder

et al. 2000

Photochem Photobiol

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“…The factors governing the sensitivity to photolysis of tryptophan (trp)t residues in proteins are a subject of interest and investigation. The polarity of the microenvironment in which the trp residue is placed is important in its photolability (Grossweiner, 1976;Grossweiner et al, 1982). It has been suggested that the nature of the neighboring residue is important to the process as well (Tassin and Borkman, 1980).…”

Section: Introductionmentioning

confidence: 99%

THE CONFORMATIONAL STATUS OF A PROTEIN INFLUENCES THE AEROBIC PHOTOLYSIS OF ITS TRYPTOPHAN RESIDUES: MELITTIN, β‐ LACTOGLOBULIN and THE CRYSTALLINS

Rao

Balasubramanian

1990

Photochem & Photobiology

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We have studied the aerobic photolysis of the tryptophan residues of the proteins melittin and beta-lactoglobulin when the proteins are in ordered conformations and when they are in randomly coiled states. The results suggest that the conformational status of the protein is a factor that influences the photolysis of the constituent tryptophan residues. This point appears to be of relevance to the photo-oxidation of the tryptophan residues of the eye lens proteins crystallins.

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“…residues in proteins was studied earlier on three proteins containing a single TRP residue more or less accessible to aqueous medium (Pigault and Gerard, 1984). As in other publications (Grossweiner, 1976(Grossweiner, , 1982, the polarity of the local microenvironment was shown to be an essential factor in determining the photolability of a residue in proteins. On the other hand, results obtained with melittin, a polypeptide whose single tryptophan could be in various environments according to the aggregation state, were not obvious and suggested that interactions between the monomeric chains could modify the photolysis rate.…”

Section: Introductionmentioning

confidence: 74%

Photolysis of the Single Tryptophan Residue of Eel Troponin C

Pigault¹,

Gérard²

1988

Photochem & Photobiology

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The tryptophan (TRP) residue of eel troponin C was selectively degraded by direct UV irradiation, at 302 nm, in Ar-saturated solution. Depending on the absence or presence of calcium ions, this TRP residue is exposed to aqueous medium or buried in a hydrophobic environment. Tryptophan loss was determined by both absorption and fluorescence spectroscopy and by amino acid analysis. The photodegradation yield was significantly higher for the exposed TRP residue than for the buried ones. These results give more detail on previous observations on several other proteins and corroborate the predominant influence of the polarity on the photosensitivity of a TRP residue in polypeptidic structures

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Primary Processes in the Photochemistry of Proteins

Cited by 14 publications

References 30 publications

The Dose Dependence of Cyclobutane Dimer Induction and Repair in UVB-irradiated Human Keratinocytes¶

The Dose Dependence of Cyclobutane Dimer Induction and Repair in UVB-irradiated Human Keratinocytes¶

THE CONFORMATIONAL STATUS OF A PROTEIN INFLUENCES THE AEROBIC PHOTOLYSIS OF ITS TRYPTOPHAN RESIDUES: MELITTIN, β‐ LACTOGLOBULIN and THE CRYSTALLINS

Photolysis of the Single Tryptophan Residue of Eel Troponin C

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