Static and time-resolved absorption spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: evidence for an equilibrium between bR570 and an O-like species.

doi:10.1021/bi00060a019

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Article

Static and time-resolved absorption spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: evidence for an equilibrium between bR570 and an O-like species.

Biochemistry - 9 Mar 1993

Sonar S, Krebs M P, Khorana H G, Rothschild K J

Abstract excerpt

The light-dark adaptation, photocycle kinetics, and acid-induced blue formation of the bacteriorhodopsin (bR) mutant Tyr-185-->Phe (Y185F) expressed in Halobacterium halobium have been investigated by both static and time-resolved visible absorption spectroscopy. Evidence is presented that a pH-d...

Topics

Bacteriorhodopsins
Darkness
Halobacterium salinarum
Hydrogen-Ion Concentration
Light
Mutation
Osmolar Concentration
Phenylalanine
Spectrophotometry, Ultraviolet
Tyrosine

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