Alkylated Hydroxylamine Derivatives Eliminate Peripheral Retinylidene Schiff Bases but Cannot Enter the Retinal Binding Pocket of Light-Activated Rhodopsin

Biochemistry ◽  
2011 ◽  
Vol 50 (33) ◽  
pp. 7168-7176 ◽  
Author(s):  
Ronny Piechnick ◽  
Martin Heck ◽  
Martha E. Sommer
Keyword(s):  
Schiff Bases ◽  
Binding Pocket ◽  
Hydroxylamine Derivatives ◽  
Retinal Binding Pocket

Steric constraints in the retinal binding pocket of sensory rhodopsin I

Biochemistry ◽  
1993 ◽  
Vol 32 (38) ◽  
pp. 10224-10232 ◽  
Author(s):  
Bing Yan ◽  
Aihua Xie ◽  
G. Ulrich Nienhaus ◽  
Yuko Katsuta ◽  
John L. Spudich
Keyword(s):  
Binding Pocket ◽  
Sensory Rhodopsin ◽  
Sensory Rhodopsin I ◽  
Retinal Binding Pocket ◽  
Steric Constraints

scholarly journals Conserved amino acids in F-helix of bacteriorhodopsin form part of a retinal binding pocket

FEBS Letters ◽  
1989 ◽  
Vol 250 (2) ◽  
pp. 448-452 ◽  
Author(s):  
K.J. Rothschild ◽  
M.S. Braiman ◽  
T. Mogi ◽  
L.J. Stern ◽  
H.G. Khorana
Keyword(s):  
Amino Acids ◽  
Binding Pocket ◽  
Form Part ◽  
Retinal Binding Pocket ◽  
Conserved Amino Acids

scholarly journals Probing a Polar Cluster in the Retinal Binding Pocket of Bacteriorhodopsin by a Chemical Design Approach

PLoS ONE ◽  
2012 ◽  
Vol 7 (8) ◽  
pp. e42447 ◽  
Author(s):  
Rosana Simón-Vázquez ◽  
Marta Domínguez ◽  
Víctor A. Lórenz-Fonfría ◽  
Susana Álvarez ◽  
José-Luís Bourdelande ◽  
...  
Keyword(s):  
Binding Pocket ◽  
Design Approach ◽  
Polar Cluster ◽  
Chemical Design ◽  
Retinal Binding Pocket

scholarly journals Time-Resolved Ultraviolet Resonance Raman of Protein Structural Changes in The KI-Intermediate Of Bacteriorhodopsin

1999 ◽  
Vol 19 (1-4) ◽  
pp. 165-168 ◽  
Author(s):  
Shoji Kaminaka ◽  
Richard A. Mathies
Keyword(s):  
Structural Changes ◽  
Resonance Raman ◽  
Difference Spectrum ◽  
Binding Pocket ◽  
Stray Light ◽  
Time Resolved ◽  
Ultraviolet Resonance Raman ◽  
Transient Intermediates ◽  
Retinal Binding Pocket ◽  
Low Dispersion

To obtain high quality time-resolved ultraviolet resonance Raman (UVRR) spectra of transient intermediates in the bacteriorhodopsin (BR) photocycle, we developed a new UVRR spectrometer. A home-made F=3.5 prism prefilter was used in front of a 50 cm CCD detected spectrograph to give high throughput, wide tunability, and excellent stray light rejection along with low dispersion. Using this system, we obtained 239.5 nm excited time-resolved UVRR spectra of BR which revealed small but significant features associated with the formation of the KL-intermediate at 10 ns delays. This difference spectrum exhibits intensity decreases at 1624, 1561, 1012 and 763cm-1 due to an altered environment of one or more Trp residues and a frequency shift of the Tyr ʋ8b band at 1602 cm-1. These signals show that the photoisomerization of retinal from all-trans to 13-cis induces significant changes in the structure and environment of aromatic residues that line the retinal binding pocket in only 10 ns.

Characterization of an opsin gene from the ascomycete Leptosphaeria maculans

Genome ◽  
2001 ◽  
Vol 44 (2) ◽  
pp. 167-171 ◽  
Author(s):  
Alexander Idnurm ◽  
Barbara J Howlett
Keyword(s):  
Leptosphaeria Maculans ◽  
Brassica Species ◽  
Binding Pocket ◽  
Opsin Gene ◽  
Amino Acid Residues ◽  
Blackleg Disease ◽  
Type Locus ◽  
Cloned Gene ◽  
Retinal Binding Pocket

An opsin gene (ops) has been characterized from Leptosphaeria maculans, the ascomycete that causes blackleg disease of Brassica species. This is the second opsin identified outside the archaeal and animal kingdoms. The gene encodes a predicted protein with high similarity (70.3%) and identity (53.3%) to the nop-1 opsin of another ascomycete Neurospora crassa. The L. maculans opsin also has identical amino acid residues in 20 of the 22 residues in the retinal-binding pocket of archaeal opsins. Opsin, on the fourth largest chromosome of L. maculans and 22 cM from the mating type locus, is the first cloned gene to be mapped in L. maculans. Opsin is transcribed at high levels in mycelia grown in the presence and absence of light; this pattern is in contrast with that of the N. crassa opsin, which is transcribed only in the light.Key words: opsin, Phoma lingam, Brassica napus.

Noncovalent occupancy of the retinal-binding pocket of opsin diminishes bleaching adaptation of retinal cones

Neuron ◽  
1993 ◽  
Vol 11 (3) ◽  
pp. 513-522 ◽  
Author(s):  
Jing Jin ◽  
Rosalie K. Crouch ◽  
D.Wesley Corson ◽  
Bernice M. Katz ◽  
Edward F. MacNichol ◽  
...  
Keyword(s):  
Binding Pocket ◽  
Retinal Binding Pocket

An Amino Acid Residue (S201) in the Retinal Binding Pocket Regulates the Photoreaction Pathway of Phoborhodopsin

Biochemistry ◽  
2011 ◽  
Vol 50 (33) ◽  
pp. 7177-7183 ◽  
Author(s):  
Gang Dai ◽  
Yu Zhang ◽  
Jun Tamogami ◽  
Makoto Demura ◽  
Naoki Kamo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Binding Pocket ◽  
Retinal Binding Pocket

CNDOL: A fast and reliable method for the calculation of electronic properties of very large systems. Applications to retinal binding pocket in rhodopsin and gas phase porphine

2007 ◽  
Vol 127 (14) ◽  
pp. 145102 ◽  
Author(s):  
Luis Alberto Montero-Cabrera ◽  
Ute Röhrig ◽  
Juan A. Padrón-Garcia ◽  
Rachel Crespo-Otero ◽  
Ana L. Montero-Alejo ◽  
...  
Keyword(s):  
Electronic Properties ◽  
Gas Phase ◽  
Reliable Method ◽  
Binding Pocket ◽  
Large Systems ◽  
Retinal Binding Pocket

scholarly journals Unique Retinal Binding Pocket of Primate Blue-Sensitive Visual Pigment

Biochemistry ◽  
2020 ◽  
Vol 59 (28) ◽  
pp. 2602-2607
Author(s):  
Yuki Nonaka ◽  
Shunpei Hanai ◽  
Kota Katayama ◽  
Hiroo Imai ◽  
Hideki Kandori
Keyword(s):  
Visual Pigment ◽  
Binding Pocket ◽  
Retinal Binding Pocket
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