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Biophysical Journal 67: 1173-1178 (1994)
© 1994 the Biophysical Society

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Two progressive substrates of the M-intermediate can be identified in glucose-embedded, wild-type bacteriorhodopsin.

J Vonck, B G Han, F Burkard, G A Perkins and R M Glaeser

Life Sciences Division, Donner Laboratory, Lawrence Berkeley Laboratory, Berkeley, California 94720.

ABSTRACT

Glucose-embedded bacteriorhodopsin shows M-intermediates with different Amide I infrared bands when samples are illuminated at 240 or 260 K, in contrast with fully hydrated samples where a single M-intermediate is formed at all temperatures. In hydrated, but not in glucose-embedded specimens, the N intermediate is formed together with M at 260 K. Both Fourier transform infrared and electron diffraction data from glucose-embedded bacteriorhodopsin suggest that at 260 K a mixture is formed of the M-state that is trapped at 240 K, and a different M-intermediate (MN) that is also formed by mutant forms of bacteriorhodopsin that lack a carboxyl group at the 96 position, necessary for the M to N transition. The fact that an MN species is trapped in glucose-embedded, wild-type bacteriorhodopsin suggests that the glucose samples lack functionally important water molecules that are needed for the proton transfer aspartate 96 to the Schiff base (and, thus, to form the N-intermediate); thus, aspartate 96 is rendered ineffective as a proton donor.




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H. Kamikubo and M. Kataoka
Can the Low-Resolution Structures of Photointermediates of Bacteriorhodopsin Explain Their Crystal Structures?
Biophys. J., March 1, 2005; 88(3): 1925 - 1931.
[Abstract] [Full Text] [PDF]


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Copyright © 1994 by the Biophysical Society.