Effects of Mutations of Lys41 and Asp102 of Bacteriorhodopsin

Zhao, Yingchun; Wang, Yazhuo; Ma, Da; Jia, Wang; Huang, Weida; Ding, Jiandong

doi:10.1271/bbb.110180

Cited by 7 publications

(4 citation statements)

References 45 publications

(39 reference statements)

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“…An earlier study has found that the sole expression of BR gene in the strain L33 without any mutation result in no significant variance in the p K a of PRC in the M state (24). However, our P77D mutant exhibits proton pumping behavior with features in between the wild‐type BR and AR4 (Fig.…”

Section: Discussionmentioning

confidence: 98%

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Effect of Substitution of Proline‐77 to Aspartate on the Light‐Driven Proton Release of Bacteriorhodopsin

Wang

Zhao

Ming

et al. 2012

Photochem & Photobiology

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Wild-type bacteriorhodopsin (BR) and another retinal protein archaerhodopsin 4 (AR4) are both light-driven proton pumps, but exhibit opposite temporal orders of proton release and uptake upon a flash illumination at neutral pH due to a higher pK(a) of proton release complex (PRC) in AR4. Since the 77th residue in the extracellular side is proline (P) in BR, but aspartic acid (D) in AR4, we have mutated P77 in BR by D in this study. The new point mutation was found to affect the kinetics of proton release and the pH dependence significantly. Upon a flash excitation, three components "fast proton release,""proton uptake" and "slow proton release" were observed at neutral pH in P77D. The pK(a) of PRC in the M intermediate was increased from 5.6 in the wild-type to 7.0, and became closer to that in AR4, which is 8.4. The coupling strength between D85 and PRC were also weakened, as expected. These data indicate that the 77th residue in AR4 greatly account for the difference between the two proton pumps.

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Section: Discussionmentioning

confidence: 98%

“…Site-directed mutagenesis of BR. Gene engineering of BR-P77D was conducted according to the method by Ni et al (23,24). The BR-P77D bop gene was expressed in H. salinarium strain L33.…”

Section: Methodsmentioning

confidence: 99%

Effect of Substitution of Proline‐77 to Aspartate on the Light‐Driven Proton Release of Bacteriorhodopsin

Wang

Zhao

Ming

et al. 2012

Photochem & Photobiology

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“…For photo sensors, however, the lifetime of the signaling state(s) should be long enough to efficiently transduce the light signal to the transducer protein. It has been reported that many amino acid residues in the proton‐conducting channel or near the retinal Schiff base have crucial effects on the photocycle of proton pumps . Nevertheless, the effects of amino acid residues that are not situated in the proton‐conducting channel or are far from the retinal Schiff base have received less attention.…”

Section: Discussionmentioning

confidence: 99%

“…The amino acid sequence identities of He AR with AR1 and BR are 94% and 57%, respectively. All key functional amino acid residues of BR are conserved in He AR, including the transmembrane Asp, Glu and Arg residues associated with proton transport .…”

Section: Introductionmentioning

confidence: 99%

Two Consecutive Polar Amino Acids at the End of Helix E are Important for Fast Turnover of the Archaerhodopsin Photocycle

Geng

Dai

Chao

et al. 2019

Photochem & Photobiology

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Archaerhodopsins (ARs) is one of the members of microbial rhodopsins. Threonine 164 (T164) and serine 165 (S165) residues of the AR from Halorubrum sp. ejinoor (HeAR) are fully conserved in ARs, although they are far from the proton transfer channel and the retinal Schiff base, and are likely involved in a hydrogen-bonding network at the end of the Helix E where most microbial rhodopsins assume a "bent structure". In the present work, T164 and/or S165 were replaced with an alanine (A), and the photocycles of the mutants were analyzed with flash photolysis. The amino acid replacements caused profound changes to the photocycle of HeAR including prolonged photocycle, accelerated decay of M intermediate and appearance of additional two intermediates which were evident in T164A-and T164A/S165A-HeAR photocyles. These results suggest that although T164 and S165 are located at the far end of the photoactive center, these two amino acid residues are important for maintaining the fast turnover of the HeAR photocycle. The underlying molecular mechanisms are discussed in relation to hydrogenbonding networks involving these two amino acids. Present study may arouse our interests to explore the functional role of the well-conserved "bent structure" in different types of microbial rhodopsin.

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Cell–Material Interactions Revealed Via Material Techniques of Surface Patterning

2013

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Cell-material interactions constitute a key fundamental topic in biomaterials study. Various cell cues and matrix cues as well as soluble factors regulate cell behaviors on materials. These factors are coupled with each other as usual, and thus it is very difficult to unambiguously elucidate the role of each regulator. The recently developed material techniques of surface patterning afford unique ways to reveal the underlying science. This paper reviews the pertinent material techniques to fabricate patterns of microscale and nanoscale resolutions, and corresponding cell studies. Some issues are emphasized, such as cell localization on patterned surfaces of chemical contrast, and effects of cell shape, cell size, cell-cell contact, and seeding density on differentiation of stem cells. Material cues to regulate cell adhesion, cell differentiation and other cell events are further summed up. Effects of some physical properties, such as surface topography and matrix stiffness, on cell behaviors are also discussed; nanoscaled features of substrate surfaces to regulate cell fate are summarized as well. The pertinent work sheds new insight into the cell-material interactions, and is stimulating for biomaterial design in regenerative medicine, tissue engineering, and high-throughput detection, diagnosis, and drug screening.

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Effects of Mutations of Lys41 and Asp102 of Bacteriorhodopsin

Cited by 7 publications

References 45 publications

Effect of Substitution of Proline‐77 to Aspartate on the Light‐Driven Proton Release of Bacteriorhodopsin

Effect of Substitution of Proline‐77 to Aspartate on the Light‐Driven Proton Release of Bacteriorhodopsin

Two Consecutive Polar Amino Acids at the End of Helix E are Important for Fast Turnover of the Archaerhodopsin Photocycle

Cell–Material Interactions Revealed Via Material Techniques of Surface Patterning

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