Photochemistry of Modified Proteins Benzophenone‐containing Bovine Serum Albumin

Mariano, Patrick S.; Glover, George I.; Wilkinson, Timothy J.

doi:10.1111/j.1751-1097.1976.tb07235.x

Cited by 6 publications

(2 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The observations summarized in the Results section indicate that the modified BSA' s prepared by the reaction of BSA with p-benzoylbenzyl bromide under a variety of conditions undergo intraprotein photochemical reactions upon selective excitation of the covalently bound benzophenone moieties. Although the exact structural outcome of this process is unknown, it appears reasonable that the photochemical reactivity of these proteins parallels closely that of the earlier studied p-benzoylphenylacetimido-BSA system (Mariano et a/., 1976a). Accordingly, the present experimental findings can be conveniently rationalized on the basis of intraprotein photoreactions in which hydrogen atom abstractions by the triplet excited benzophenone groups results in a localized radical pair which couples to form benzhydrol linkages (Scheme 4).…”

Section: Modified Protein Photoreactionssupporting

confidence: 67%

AFFINITY‐CONTROLLED TRIPLET ENERGY TRANSFER FROM p‐BENZOYLBENZYL‐BOVINE SERUM ALBUMIN TO LOW MOLECULAR WEIGHT QUENCHERS

Glover

Mariano

Hildreth

1978

Photochem & Photobiology

Self Cite

View full text Add to dashboard Cite

Abstract— Methods for the controlled synthesis of modified protein photosensitizers which maximize affinity‐controlled energy transfer are discussed. Modified proteins containing covalently linked benzophenone groups were prepared by the reaction of bovine serum albumin with p‐benzoylbenzyl bromide under conditions limiting the number and locations of the introduced benzophenone chromophores. The mechanism of energy transfer responsible for quenching of triplet photochemical reactions of the modified proteins was explored using water soluble quenchers. In addition, methods were employed to determine the magnitude of the contribution of the affinity‐controlled mechanism for energy transfer in these systems. The utility of sodium‐cis‐8‐methylene‐4,9‐decadienoate as a triplet energy transfer indicator for macromolecular systems was demonstrated using the modified proteins as sensitizers. The trienoic acid was prepared starting with the known 4‐methylene‐5‐hexenal by the Wittig reaction with 3‐ethoxycarbonylpropylidene triphenylphosphorane followed by saponification. Triplet sensitized irradiation of this trienoic acid using p‐benzoylbenzyltriethylammonium chloride as sensitizer led to production of endo‐ and exo‐1‐vinyl‐5‐(3‐carboxyethyl)bicyclo[2.1.1]hexane along with the trans acid. Characterization of the bicyclohexane products was made on the basis of spectroscopic evidence. Results demonstrate that quenching of the intramolecular photoreactions of the modified proteins by trienoic acid must be a result of triplet energy transfer, since irradiation of these modified proteins in the presence of the trienoic acid salt led to the characteristic triplet photoproduct mixture.

show abstract

Section: Modified Protein Photoreactionssupporting

confidence: 67%

AFFINITY‐CONTROLLED TRIPLET ENERGY TRANSFER FROM p‐BENZOYLBENZYL‐BOVINE SERUM ALBUMIN TO LOW MOLECULAR WEIGHT QUENCHERS

Glover

Mariano

Hildreth

1978

Photochem & Photobiology

Self Cite

View full text Add to dashboard Cite

show abstract

“…Other Reagents. An imidate-functionalized BP (38) was among the first reagents employed for protein modification (Mariano et al, 1976). The [3H]BZDC reagent (39) was discussed in detail in the Biochemical Applications of Tethered Benzophenones section above and was first developed for IP3R labeling (Mourey et al, 1993).…”

Section: Site-directed Photolabeling With Polypeptides Containing 4-b...mentioning

confidence: 99%

Benzophenone Photophores in Biochemistry

1994

View full text Add to dashboard Cite

The photoactivatable aryl ketone derivatives have been rediscovered as biochemical probes in the last 5 years. The expanding use of benzophenone (BP) photoprobes can be attributed to three distinct chemical and biochemical advantages. First, BPs are chemically more stable than diazo esters, aryl azides, and diazirines. Second, BPs can be manipulated in ambient light and can be activated at 350-360 nm, avoiding protein-damaging wavelengths. Third, BPs react preferentially with unreactive C-H bonds, even in the presence of solvent water and bulk nucleophiles. These three properties combine to produce highly efficient covalent modifications of macromolecules, frequently with remarkable site specificity. This Perspectives includes a brief review of BP photochemistry and a selection of specific applications of these photoprobes, which address questions in protein, nucleic acid, and lipid biochemistry.

show abstract

Mapping the Three-Dimensional Structure of Proteins by Photochemical Techniques

Jori

Spikes

1978

Photochemical and Photobiological Reviews

View full text Add to dashboard Cite

Photochemistry of Modified Proteins Benzophenone‐containing Bovine Serum Albumin

Cited by 6 publications

References 24 publications

AFFINITY‐CONTROLLED TRIPLET ENERGY TRANSFER FROM p‐BENZOYLBENZYL‐BOVINE SERUM ALBUMIN TO LOW MOLECULAR WEIGHT QUENCHERS

AFFINITY‐CONTROLLED TRIPLET ENERGY TRANSFER FROM p‐BENZOYLBENZYL‐BOVINE SERUM ALBUMIN TO LOW MOLECULAR WEIGHT QUENCHERS

Benzophenone Photophores in Biochemistry

Mapping the Three-Dimensional Structure of Proteins by Photochemical Techniques

Contact Info

Product

Resources

About