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.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Vonck J,Han BG,Burkard F,Perkins GA,Glaeser RMdoi
10.1016/S0006-3495(94)80585-5subject
Has Abstractpub_date
1994-09-01 00:00:00pages
1173-8issue
3eissn
0006-3495issn
1542-0086pii
S0006-3495(94)80585-5journal_volume
67pub_type
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