Proton Affinity Changes Driving Unidirectional Proton Transport in the Bacteriorhodopsin Photocycle

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Proton affinity changes driving unidirectional proton transport in the bacteriorhodopsin photocycle.

Bacteriorhodopsin is the smallest autonomous light-driven proton pump. Proposals as to how it achieves the directionality of its trans-membrane proton transport fall into two categories: accessibility-switch models in which proton transfer pathways in different parts of the molecule are opened and closed during the photocycle, and affinity-switch models, which focus on changes in proton affinit...

متن کامل

A correlation between proton pumping and the bacteriorhodopsin photocycle.

In an attempt to establish a relationship between proton pumping and the photocycle intermediates of bacteriorhodopsin, we have studied the effects of pH and temperature on flash-induced proton pumping and the photointermediates O640 and M412. The relative quantum yield of flash-induced proton pumping is both pH and temperature dependent. It is high in the acid pH range and at low temperatures ...

متن کامل

Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle.

In the photocycle of bacteriorhodopsin at pH 7, a proton is ejected to the extracellular medium during the protonation of Asp-85 upon formation of the M intermediate. The group that releases the ejected proton does not become reprotonated until the prephotolysis state is restored from the N and O intermediates. In contrast, at acidic pH, this proton release group remains protonated to the end o...

متن کامل

Protein conformational changes in the bacteriorhodopsin photocycle.

We report a comprehensive electron crystallographic analysis of conformational changes in the photocycle of wild-type bacteriorhodopsin and in a variety of mutant proteins with kinetic defects in the photocycle. Specific intermediates that accumulate in the late stages of the photocycle of wild-type bacteriorhodopsin, the single mutants D38R, D96N, D96G, T46V, L93A and F219L, and the triple mut...

متن کامل

Time-course and stoichiometry of fight-induced proton release and uptake during the photocycle of bacteriorhodopsin

The kinetics and stoi~hiometry of lint-indu~d proton release in purple membrane sus~nsions have been investigated using the pH-indicator dye pyranine and sin~5tu~over flash spectroscopy at a time resolution of 0.1 ps. The number of protons detected by pyranine is inversely proportional to the buffehng power of the medium and 1.1 f 0.2 protons are released per photocycling bacteriorhodopsin mole...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Journal of Molecular Biology

سال: 2003

ISSN: 0022-2836

DOI: 10.1016/s0022-2836(03)00903-3