Environmental effects on the protonation states of active site residues in bacteriorhodopsin.

Abstract:

:Finite difference solutions of the Poisson-Boltzmann equation are used to calculate the pKa values of the functionally important ionizable groups in bacteriorhodopsin. There are strong charge-charge interactions between the residues in the binding site leading to the possibility of complex titration behavior. Structured water molecules, if they exist in the binding site, can have significant effects on the calculated pKa by strongly stabilizing ionized species. The ionization states of the Schiff base and Asp-85 are found to be strongly coupled. Small environmental changes, which might occur as a consequence of trans-cis isomerization, are capable of causing large shifts in the relative pKa values of these two groups. This provides an explanation for the protonation of Asp-85 and the deprotonation of the Schiff base in the M state of bacteriorhodopsin. The different behavior of Asp-85 and Asp-212 is discussed in this regard.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Sampogna RV,Honig B

doi

10.1016/S0006-3495(94)80925-7

subject

Has Abstract

pub_date

1994-05-01 00:00:00

pages

1341-52

issue

5

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(94)80925-7

journal_volume

66

pub_type

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