Trp86 --> Phe replacement in bacteriorhodopsin affects a water molecule near Asp85 and light adaptation.

doi:10.1021/bi970081k

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Article

Trp86 --> Phe replacement in bacteriorhodopsin affects a water molecule near Asp85 and light adaptation.

Biochemistry - 6 May 1997

Hatanaka M, Kashima R, Kandori H, Friedman N, Sheves M, Needleman R, Lanyi J K, Maeda A

Abstract excerpt

Illumination of the Trp86 --> Phe mutant of bacteriorhodopsin causes anomalous light adaptation, i.e., isomerization of the retinal from all-trans to 13-cis, 15-syn. FTIR spectral analysis shows that illumination at 250 K yields two 13-cis photoproducts, the conventional 13-cis, 15-syn state, BR(...

Topics

Aspartic Acid
Bacteriorhodopsins
Halobacterium
Light
Mutation
Phenylalanine
Photochemistry
Protein Binding
Retinaldehyde
Spectroscopy, Fourier Transform Infrared
Tryptophan
Water

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