Abstract:
:The individual tryptophanyl contributions to the near-ultraviolet dichroic activity of apomyoglobin in its native conformation have been resolved. This was accomplished by comparing the spectra of two classes of apomyoglobin with different aromatic residue contents and observing the effect of a specific modification of indole residues. The circular dichroism (CD) spectra of apomyoglobins containing two tryptophanyl residues, i.e. Trp A-5 and A-12, show the presence of a positive peak centered at 292 nm, attributable to indolic chromophore, which is missing in the CD spectrum of tuna apomyoglobin possessing only Trp A-12. Moreover, the specific modification of Trp A-5 by 2-hydroxy-5-nitrobenzyl bromide is shown by the lack of the 292 nm peak and the appearance of a positive band at longer wavelength. The pH dependence of the position of this band suggests that it arises from the 2-hydroxy-5-nitrobenzyl moiety. The results suggest that Trp A-12 does not substantially contribute to the optical activity in the near ultraviolet.
journal_name
Photochem Photobioljournal_title
Photochemistry and photobiologyauthors
Sirangelo I,Irace G,Bismuto Edoi
10.1111/j.1751-1097.1994.tb09664.xsubject
Has Abstractpub_date
1994-06-01 00:00:00pages
611-4issue
6eissn
0031-8655issn
1751-1097journal_volume
59pub_type
杂志文章abstract::A new type of photochromic molecule that can be used for diffusion coefficient (D) measurements of various proteins in solution is described. The absorption spectrum of this molecule is changed upon photoexcitation by the trans-cis isomerization reaction. Target proteins were labeled by this photochromic molecule in t...
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