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Molecular mechanism of vectorial proton translocation by bacteriorhodopsin

Molecular mechanism of vectorial proton translocation by bacteriorhodopsin

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_762280734

Molecular mechanism of vectorial proton translocation by bacteriorhodopsin

About this item

Full title

Molecular mechanism of vectorial proton translocation by bacteriorhodopsin

Publisher

London: Nature Publishing Group UK

Journal title

Nature (London), 2000-08, Vol.406 (6796), p.653-657

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Bacteriorhodopsin, a membrane protein with a relative molecular mass of 27,000, is a light driven pump which transports protons across the cell membrane of the halophilic organism
Halobacterium salinarum
. The chromophore retinal is covalently attached to the protein via a protonated Schiff base. Upon illumination, retinal is isomerized. The...

Alternative Titles

Full title

Molecular mechanism of vectorial proton translocation by bacteriorhodopsin

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_762280734

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_762280734

Other Identifiers

ISSN

0028-0836

E-ISSN

1476-4687

DOI

10.1038/35020614

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