Direct observation of the PH-dependent equilibrium between L-like and M intermediates of photoactive yellow protein

被引：19

作者：

Imamoto, Y ^{[1
]}

Harigal, M ^{[1
]}

Kataoka, M ^{[1
]}

机构：

[1] Nara Inst Sci & Technol, Grad Sch Mat Sci, Nara 6300192, Japan

来源：

FEBS LETTERS | 2004年 / 577卷 / 1-2期

关键词：

photoreaction cycle; intermediate; PAS domain; conformational change; pH titration;

D O I：

10.1016/j.febslet.2004.09.065

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Equilibrium between the photoproducts of photoactive yellow protein (PYP), present in a millisecond time scale, was studied. The near-UV intermediate of PYP (PYPM) was red-shifted by alkalization due to the deprotonation of the chromophore (pK(a) = 10.2). In addition, a small amount of red-shifted intermediate coexisted with PYPM. Its spectral shape in the visible region agreed with that Of PYPL, the precursor of PYPM. The fraction Of PYPL-like product was maximal at pH 10. It decays with a rate constant identical to that of PYPM. These results indicate that PYPL-like product is in pH-dependent equilibrium with PYPM and deprotonated PYPM. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：75 / 80

页数：6

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