About: Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation

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About: Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation Goto Sponge NotDistinct Permalink

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scientific article published on February 1990

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rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) bài báo khoa học (vi) article scientifique (fr) наукова стаття, опублікована в лютому 1990 (uk) artículu científicu espublizáu en 1990 (ast) 1990年學術文章 (zh) مقالة علمية نشرت في فبراير 1990 (ar) scientific article published on February 1990 (en)
publication date	wds:Q37684251-F6C05BD7-0087-4721-B00D-58E8119446AE
publication date	1990-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37684251-74123AFB-AFB8-49A1-9DBF-D550944046DF
language of work or name	English
cites work	wds:Q37684251-04E1B4F9-2FB4-4AD9-89DC-74960969107E wds:Q37684251-07848850-BB0E-43B8-833C-CBE10C3030BC wds:Q37684251-096DF4D7-FAA9-4660-A2EF-C452B86661ED wds:Q37684251-100A115B-DB69-4C9B-B583-AC31FA3AD75D wds:Q37684251-11577E4B-6F1E-477F-9EB2-29305B50BA0C wds:Q37684251-15261108-64DE-4B5B-A8B8-5645EF0FC050 wds:Q37684251-1D5796E4-B46C-44E4-A1F6-34C556B052F9 wds:Q37684251-2EF94B9F-8D2A-42FE-90B6-B52FDA55289A wds:Q37684251-4050FF74-9F42-4923-ADDB-D0607B03E391 wds:Q37684251-47D98316-FEE6-4327-9214-F76785EA93EA wds:Q37684251-53BB2F5E-1E56-45FC-8B6C-B8B9CE2794FF wds:Q37684251-56BEE570-4E46-4ACC-9B5B-62C3A8C3F6E0 wds:Q37684251-57F0846A-A380-40C1-8554-E620124358A7 wds:Q37684251-597D2905-FED4-4C87-9899-617FAC91559E wds:Q37684251-76701F91-86CE-4251-8FBC-2B95711E3F27 wds:Q37684251-8C94C0A3-6E8E-45BF-8279-53DE4A2721E1 wds:Q37684251-98F1B12F-3E2C-4476-A83A-8684A92C802E wds:Q37684251-9DA9DA38-262C-45AC-8043-A97E484B4AB0 wds:Q37684251-AF625838-5405-4CD9-8969-8B45E2D77F51 wds:Q37684251-CA47233E-E617-4D91-B02C-AAFF5CB1A8F2 wds:Q37684251-D0FA6780-66C2-4AE9-8EFF-3804ED330626 wds:Q37684251-D31A15F2-FABC-4A9E-9B5B-AF536CF64BBE wds:Q37684251-DF60F9A6-4BC1-4398-8F32-7054BD268B52 wds:Q37684251-FDF8B3DD-49EC-460A-ACD4-66DF0BB56F97
cites work	Fast stages of photoelectric processes in biological membranes. I. Bacteriorhodopsin Controlling the pKa of the bacteriorhodopsin Schiff base by use of artificial retinal analogues Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base Replacement of aspartic residues 85, 96, 115, or 212 affects the quantum yield and kinetics of proton release and uptake by bacteriorhodopsin. Aspartic acid substitutions affect proton translocation by bacteriorhodopsin Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin Structure-function studies on bacteriorhodopsin. IX. Substitutions of tryptophan residues affect protein-retinal interactions in bacteriorhodopsin Structure-function studies on bacteriorhodopsin. IV. Purification and renaturation of bacterio-opsin polypeptide expressed in Escherichia coli. Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212 Structure-function studies on bacteriorhodopsin. X. Individual substitutions of arginine residues by glutamine affect chromophore formation, photocycle, and proton translocation Surface pH controls purple-to-blue transition of bacteriorhodopsin. A theoretical model of purple membrane surface Cation binding by bacteriorhodopsin Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin Chromophore equilibria in bacteriorhodopsin Salt and pH-dependent changes of the purple membrane absorption spectrum Chromophore/protein and chromophore/anion interactions in halorhodopsin The purple to blue transition of bacteriorhodopsin is accompanied by a loss of the hexagonal lattice and a conformational change. Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump Reconstitution of Biological Molecular generators of electric current. Bacteriorhodopsin Proton transport by bacteriorhodopsin through an interface film Delipidation of bacteriorhodopsin and reconstitution with exogenous phospholipid. Effects of anion binding on the deprotonation reactions of halorhodopsin
author name string	wds:Q37684251-42786B89-27C4-4735-9BD6-5EA42DCEB3A3 wds:Q37684251-EE946C66-AFEB-4DBF-B361-60EE187383F6 wds:Q37684251-FFF3ED1C-7498-4505-9CAF-EFB352D89EB8
author name string	S Subramaniam H G Khorana T Marti
rdfs:label	Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation (en) Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation (ast) Protonation state of Asp (nl)
skos:prefLabel	Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation (en) Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation (ast) Protonation state of Asp (nl)
name	Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation (en) Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation (ast) Protonation state of Asp (nl)
title	wds:Q37684251-D675C016-1F91-490E-B99C-CBC482FBC34E
title	Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation (en)
page(s)	wds:Q37684251-C2BA2EE9-C370-4FA8-B767-86C9E1854A52
page(s)	1013-1017
instance of	wds:Q37684251-E5AE980D-A72F-4F6D-B6AF-D97D753EA065
instance of	scholarly article
PubMed ID	wds:Q37684251-2D1262D9-6939-4D2C-A544-32AE95FC5BC7
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1967832
PubMed ID	1967832
published in	wds:Q37684251-8EC661CF-0874-4A25-A0A9-F9C4E1E9D2D4
published in	Proceedings of the National Academy of Sciences of the United States of America
issue	wds:Q37684251-DC6CB604-ADA7-4E07-9085-49F084FC51D1
volume	wds:Q37684251-C4E9ECAD-B7C2-426B-AB68-328264B3D30E
issue	3

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