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Direct observation of the pH-dependent equilibrium between L-like and M intermediates of photoactive yellow protein.
FEBS Lett. 2004 Nov 05; 577(1-2):75-80.FL

Abstract

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 (pKa=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.

Authors+Show Affiliations

Graduate School of Materials Science, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan. imamoto@ms.naist.jpNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15527764

Citation

Imamoto, Yasushi, et al. "Direct Observation of the pH-dependent Equilibrium Between L-like and M Intermediates of Photoactive Yellow Protein." FEBS Letters, vol. 577, no. 1-2, 2004, pp. 75-80.
Imamoto Y, Harigai M, Kataoka M. Direct observation of the pH-dependent equilibrium between L-like and M intermediates of photoactive yellow protein. FEBS Lett. 2004;577(1-2):75-80.
Imamoto, Y., Harigai, M., & Kataoka, M. (2004). Direct observation of the pH-dependent equilibrium between L-like and M intermediates of photoactive yellow protein. FEBS Letters, 577(1-2), 75-80.
Imamoto Y, Harigai M, Kataoka M. Direct Observation of the pH-dependent Equilibrium Between L-like and M Intermediates of Photoactive Yellow Protein. FEBS Lett. 2004 Nov 5;577(1-2):75-80. PubMed PMID: 15527764.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Direct observation of the pH-dependent equilibrium between L-like and M intermediates of photoactive yellow protein. AU - Imamoto,Yasushi, AU - Harigai,Miki, AU - Kataoka,Mikio, PY - 2004/08/03/received PY - 2004/09/22/revised PY - 2004/09/22/accepted PY - 2004/11/6/pubmed PY - 2005/3/3/medline PY - 2004/11/6/entrez SP - 75 EP - 80 JF - FEBS letters JO - FEBS Lett VL - 577 IS - 1-2 N2 - 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 (pKa=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. SN - 0014-5793 UR - https://www.unboundmedicine.com/medline/citation/15527764/Direct_observation_of_the_pH_dependent_equilibrium_between_L_like_and_M_intermediates_of_photoactive_yellow_protein_ DB - PRIME DP - Unbound Medicine ER -