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Light-driven proton translocation by bacteriorhodopsin reconstituted with the phenyl analog of retinal.

Abstract:

The properties of bacteriorhodopsin in which the natural cofactor, retinal (Fig. 1, I), has been replaced by the synthetic analog, phenyl retinal (Fig. 1, II), have been studied. Phenyl retinal binds at the same site as retinal and supports light-dependent transmembrane proton translocation in phospholipid vesicles that contain bacterio-opsin. This result allows us to rule out proton abstraction from the beta-ionone ring of retinal as a step in the catalytic cycle. Furthermore, phenyl retinal...

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Publication status:
Published

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Journal:
The Journal of biological chemistry
Volume:
256
Issue:
8
Pages:
3797-3801
Publication date:
1981-04-05
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:b07a937e-9cf1-4111-ac4f-82fe71ce80b3
Source identifiers:
52416
Local pid:
pubs:52416

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