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Journal ArticleDOI

Photo‐conjugation of 8–methoxypsoralen with proteins

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TLDR
8–Methoxypsoralen is shown to form a covalent conjugate with bovine serum albumin by UVA irradiation in the presence of 02.78 J/ds intensity, and this photoreaction appears to be completely different from the known 8–MOP photo‐cycloaddition reaction with DNA.
Abstract
— 8–Methoxypsoralen (8–MOP) is shown to form a covalent conjugate with bovine serum albumin (BSA) by UVA irradiation in the presence of 02. The photoreaction is shown to involve oxidation of 8–MOP itself as a first step, producing an oxidation product which reacts readily with protein. Thus, this photoreaction appears to be completely different from the known 8–MOP photo-cycloaddition reaction with DNA. Among several proteins studied, human serum albumin, histone type 11, RNAse A and lysozyme also undergo photoinduced addition by 8–MOP. Chemical modifications of various amino acid residues in BSA revealed tyrosine-OH as one of the reaction sites. Irradiation (12 h) with UVA at 1.78 J/ds intensity resulted in approximately 1.5 mot of 8–MOP bound to 1 mol of BSA.

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Citations
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Journal ArticleDOI

Photochemistry and photobiology of psoralens.

TL;DR: Photoreactions of other bases such as adenine and the mechanisms other than cycloaddition should be investigated in order to fully assess the specificity of psoralen photoreactions and their application as a probe for biopolymer structure and as a tool for photobiological studies of microorganisms.
Journal ArticleDOI

Recent advances in psoralen phototoxicity mechanism

TL;DR: The present overview outlines some of the recent research developments leading to a better understanding of the mechanisms which underlie psoralen induced phototoxicity.
Book ChapterDOI

Nonenzymatic covalent posttranslational modification of proteins in vivo

TL;DR: In vivo analysis of non-enzymatic covalent post-translational modification of proteins in vivo is presented and is subdivided according to the nature of the chemical reactions and the types of compounds binding to proteins.
Journal ArticleDOI

Molecular aspects of furocoumarin reactions: Photophysics, photochemistry, photobiology, and structural analysis

TL;DR: Furocoumarin derivatives absorb UVA light and act as photosensitizers, they have been used as helpful molecular probes and as skin disease drugs and the versatility of these compounds is entirely due to their optical properties.
Journal ArticleDOI

Photochemistry of proteins: a review.

TL;DR: Proteins are an important target of photochemical damage to the eye and N-formylkynurenine is an important tryptophan photoproduct, which can act as an endogenous photosensitizer of near-ultraviolet radiation by generating singlet oxygen and superoxide.
References
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Journal ArticleDOI

The Nature of the Amino Acid Residues Involved in the Inactivation of Ribonuclease by Iodoacetate

TL;DR: The fact, that the pH optimum for the reaction leading to the formation of imidazole carboxymethyl ribonuclease is around pH 5.5 to 6, instead of at the more alkaline pH values observed for the alkylation of cy-N-acetylhistidine, suggests that inactivation takes place as a result of substitution on a particular one of the four histidine residues present in rib onuclease.
Journal ArticleDOI

The Binding of N-Ethylmaleimide by Human Hemoglobin and Its Effect upon the Oxygen Equilibrium

TL;DR: In order to determine more fully the role of sulfhydryl groups in hemoglobin, the effects of N-ethylmaleimide are investigated, which have led to an altered picture of the nature of groups responsible for the Hf discharge which accompanies oxygenation.
Journal ArticleDOI

Photodynamic sensitization by 8-methoxypsoralen via the singlet oxygen mechanism.

TL;DR: Evidence is presented to indicate that the binding of 8-MOP to double stranded poly(dA-dT) inhibits its ability to sensitize via this mechanism, and that singlet oxygen (lo2) generated by triplet energy transfer is the principal reactive intermediate in the inactivation of lysozyme and oxidation of aqueous iodide ion.
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