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THE EFFECT OF CROSS‐LINKING ON PHOTOCYCLING ACTIVITY OF BACTERIORHODOPSIN
Author(s) -
Konishi Tetsuya,
Tristram Stephanie,
Packer Lester
Publication year - 1979
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1979.tb07058.x
Subject(s) - bacteriorhodopsin , chemistry , lysine , moiety , oligomer , halobacteriaceae , stereochemistry , intramolecular force , proteolysis , biochemistry , membrane , organic chemistry , amino acid , enzyme , halobacterium salinarum
— Purple membrane preparations from Halobacterium halobium were chemically modified with imidoesters. Dimethyl adipimidate (8.3 Å chain length) amidinates about five of the six free lysine residues whereas dimethyl suberimidate (11.3 Å) under the same conditions reacts with only 2–3 residues. Gel electrophoresis showed that the shorter chain length imidoesters were less effective than dimethyl suberimidate in oligomer formation. However, dimethyl adipimidate resulted in a more marked inhibition of the photoreaction activity. Monofunctional imidates, methyl acetimidate and methyl butyrimi‐date, at comparable degrees of amidination, did not appreciably affect activity indicating that the presence of bulky groups on the exposed lysine residues does not cause the effects observed. Hence, the introduction of molecular mobility constraints by intramolecular cross‐linking slows photocycling, and, therefore, inhibits proton pumping activity of bacteriorhodopsin. This indicates that conforma‐tional changes of the protein moiety of bacteriorhodopsin occur during photocycling activity.