BACTERIORHODOPSIN

INDHUMATHI. J
14MG05

ORIGIN AND DISCOVERY

In 1971 ,discovery was reported by
Oesterhelt and Stoeckenius.
Halobacterium halobium -Source

 Bacteriorhodopsin (BR) absorbs light

@ 570 nm (visible green light)
Red and Blue light is reflected, giving
membrane its purple color
BR functions as a proton pump

Milestones in BR Structural
Determination
In order to assess the structure and
mechanism of BR, or any membrane
protein, we really need to understand
its tertiary structure by X-ray
crystallography
BUT, membrane proteins dont
crystallize easily

Nobel Prize in Chemistry

(1988)
Hartmut

Michel
First to
crystallize BR
in 1980
Contribution
to
determination
of structure of
a
photosynthetic
reaction
center earned
him a Nobel

Findings
Could get protein crystallization
Crystals were too small and
disordered to determine tertiary
structure

1990
Henderson et al. use cryocrystallography to study BR
Crystallization occurred
First instances of structural
determination
However, some areas of the protein
could not be resolved

1990 First structure of BR

1996: E.M Landau

& J.P. Rosenbusch
Use Cubic Lipid Phase Matrix
First complete structural
determination of BR

BACTERIORHODOPSIN
Biological
macromolecule
Integral
membrane protein
Simple cell
membrane
receptor
G-protein coupled
seven helix
receptors

786 nt structural gene

248 aminoacids
No intervening sequences
24kDa

Structural Info
7 TM helices
Forms a homotrimer
Homotrimers aggregate to form the purple
membrane
Each bacteriorhodopsin contains one
molecule of a linear pigment called retinal
Stability of trimer by:
G113, I117, L48
Most stability comes from surrounding lipids

FUNCTION

The protein absorbs

green light (wavelength
500-650 nm, with the
absorption maximum at
568 nm) and converts it
into an electrochemical
gradient. This gradient in
turn is used for ATP
production. The ability of
BR to convert light energy
into chemical energy or
sunlight into electricity has
been used in different
applications mainly optical
appliances but also for
therapeutic/medical
applications and research.

STRUCTURE

RETINAL

RETINAL
The light interacting group in BR is a
retinylidene residue attached via a Schiff base
linkage to the protein moiety.
one end is attached to the nitrogen atom of a
lysine residue in helix G and the other end is
wedged deep in the protein.
Retinal changes its structure in response to
visible light.
The polypeptide harnesses the light energy
trapped by the retinal and uses it to push a
single proton through the seven-helix bundle,
from the cell interior to the outside.

MECHANISM

ISOMERISATION OF RETINAL

Thank you