Real-time spectroscopy of transition states in bacteriorhodopsin during retinal isomerization

Nature ◽  
2001 ◽  
Vol 414 (6863) ◽  
pp. 531-534 ◽  
Author(s):  
Takayoshi Kobayashi ◽  
Takashi Saito ◽  
Hiroyuki Ohtani
Keyword(s):  
Real Time ◽  
Transition States

scholarly journals Real‐time femtosecond probing of ‘‘transition states’’ in chemical reactions

1987 ◽  
Vol 87 (4) ◽  
pp. 2395-2397 ◽  
Author(s):  
Marcos Dantus ◽  
Mark J. Rosker ◽  
Ahmed H. Zewail
Keyword(s):  
Real Time ◽  
Chemical Reactions ◽  
Transition States

scholarly journals Femtosecond real-time probing of reactions. 12. Vectorial dynamics of transition states

1993 ◽  
Vol 97 (48) ◽  
pp. 12447-12459 ◽  
Author(s):  
T. Baumert ◽  
S. Pedersen ◽  
A. H. Zewail
Keyword(s):  
Real Time ◽  
Transition States

Force-activated catalytic pathway accelerates bacterial adhesion against flow

2018 ◽  
Vol 475 (16) ◽  
pp. 2611-2620 ◽  
Author(s):  
Jagadish P. Hazra ◽  
Nisha Arora ◽  
Amin Sagar ◽  
Shwetha Srinivasan ◽  
Abhishek Chaudhuri ◽  
...  
Keyword(s):  
Real Time ◽  
Single Molecule ◽  
Bacterial Adhesion ◽  
Rational Design ◽  
Enzymatic Reaction ◽  
Transition States ◽  
Factors Affecting ◽  
The Real ◽  
Time Dynamics ◽  
Dynamics Simulations

Mechanical cues often influence the factors affecting the transition states of catalytic reactions and alter the activation pathway. However, tracking the real-time dynamics of such activation pathways is limited. Using single-molecule trapping of reaction intermediates, we developed a method that enabled us to perform one reaction at one site and simultaneously study the real-time dynamics of the catalytic pathway. Using this, we showed single-molecule calligraphy at nanometer resolution and deciphered the mechanism of the sortase A enzymatic reaction that, counter-intuitively, accelerates bacterial adhesion under shear tension. Our method captured a force-induced dissociation of the enzyme–substrate bond that accelerates the forward reaction 100×, proposing a new mechano-activated catalytic pathway. In corroboration, our molecular dynamics simulations in the presence of force identified a force-induced conformational switch in the enzyme that accelerates proton transfer between CYS184 (acceptor) and HIS120 (donor) catalytic dyads by reducing the inter-residue distances. Overall, the present study opens up the possibility of studying the influence of factors affecting transition states in real time and paves the way for the rational design of enzymes with enhanced efficiency.

scholarly journals Sub-5-fs Real-time Spectroscopy of Transition States in Bacteriorhodopsin During Retinal Isomerization†

2007 ◽  
Vol 83 (2) ◽  
pp. 363-369 ◽  
Author(s):  
Takayoshi Kobayashi ◽  
Atsushi Yabushita ◽  
Takashi Saito ◽  
Hiroyuki Ohtani ◽  
Motoyuki Tsuda
Keyword(s):  
Real Time ◽  
Transition States

Some Recent Results in Quiescent Prominence Spectrometry

1979 ◽  
Vol 44 ◽  
pp. 41-47
Author(s):  
Donald A. Landman
Keyword(s):  
Real Time ◽  
Computer System ◽  
Spectral Response ◽  
Absolute Intensity ◽  
Solar Observatory ◽  
Target Size ◽  
Small Target ◽  
Signal Averaging ◽  
Quiescent Prominence

This paper describes some recent results of our quiescent prominence spectrometry program at the Mees Solar Observatory on Haleakala. The observations were made with the 25 cm coronagraph/coudé spectrograph system using a silicon vidicon detector. This detector consists of 500 contiguous channels covering approximately 6 or 80 Å, depending on the grating used. The instrument is interfaced to the Observatory’s PDP 11/45 computer system, and has the important advantages of wide spectral response, linearity and signal-averaging with real-time display. Its principal drawback is the relatively small target size. For the present work, the aperture was about 3″ × 5″. Absolute intensity calibrations were made by measuring quiet regions near sun center.

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