scholarly journals Spiers Memorial Lecture : Interplay of theory and computation in chemistry—examples from on-water organic catalysis, enzyme catalysis, and single-molecule fluctuations

2010 ◽  
Vol 145 ◽  
pp. 9-14 ◽  
Author(s):  
R. A. Marcus
2013 ◽  
Vol 104 (2) ◽  
pp. 372a
Author(s):  
Tatyana Terentyeva ◽  
Johan Hofkens ◽  
Chun-Biu Li ◽  
Kerstin Blank

2017 ◽  
Vol 205 ◽  
pp. 9-30 ◽  
Author(s):  
Anne-Isabelle Henry ◽  
Tyler W. Ueltschi ◽  
Michael O. McAnally ◽  
Richard P. Van Duyne

Four decades on, surface-enhanced Raman spectroscopy (SERS) continues to be a vibrant field of research that is growing (approximately) exponentially in scope and applicability while pushing at the ultimate limits of sensitivity, spatial resolution, and time resolution. This introductory paper discusses some aspects related to all four of the themes for this Faraday Discussion. First, the wavelength-scanned SERS excitation spectroscopy (WS-SERES) of single nanosphere oligomers (viz., dimers, trimers, etc.), the distance dependence of SERS, the magnitude of the chemical enhancement mechanism, and the progress toward developing surface-enhanced femtosecond stimulated Raman spectroscopy (SE-FSRS) are discussed. Second, our efforts to develop a continuous, minimally invasive, in vivo glucose sensor based on SERS are highlighted. Third, some aspects of our recent work in single molecule SERS and the translation of that effort to ångstrom-scale spatial resolution in ultrahigh vacuum tip-enhanced Raman spectroscopy (UHV-TERS) and single molecule electrochemistry using electrochemical (EC)-TERS will be presented. Finally, we provide an overview of analytical SERS with our viewpoints on SERS substrates, approaches to address the analyte generality problem (i.e. target molecules that do not spontaneously adsorb and/or have Raman cross sections <10−29 cm2 sr−1), SERS for catalysis, and deep UV-SERS.


Biochemistry ◽  
2005 ◽  
Vol 44 (51) ◽  
pp. 16835-16843 ◽  
Author(s):  
Nina M. Antikainen ◽  
R. Derike Smiley ◽  
Stephen J. Benkovic ◽  
Gordon G. Hammes

Author(s):  
Raul Perez-Jimenez ◽  
Jorge Alegre-Cebollada

2010 ◽  
Vol 26 (07) ◽  
pp. 1976-1987
Author(s):  
SU Xiao-Dong ◽  
◽  
◽  
JIN Jian-Shi ◽  
XIE Sunney Xiaoliang ◽  
...  

2009 ◽  
Vol 113 (6) ◽  
pp. 2393-2404 ◽  
Author(s):  
Weilin Xu ◽  
Jason S. Kong ◽  
Peng Chen

2018 ◽  
Vol 115 (39) ◽  
pp. 9738-9743 ◽  
Author(s):  
Felix Wong ◽  
Annwesha Dutta ◽  
Debashish Chowdhury ◽  
Jeremy Gunawardena

The Michaelis–Menten (MM) fundamental formula describes how the rate of enzyme catalysis depends on substrate concentration. The familiar hyperbolic relationship was derived by timescale separation for a network of three reactions. The same formula has subsequently been found to describe steady-state input–output responses in many biological contexts, including single-molecule enzyme kinetics, gene regulation, transcription, translation, and force generation. Previous attempts to explain its ubiquity have been limited to networks with regular structure or simplifying parametric assumptions. Here, we exploit the graph-based linear framework for timescale separation to derive general structural conditions under which the MM formula arises. The conditions require a partition of the graph into two parts, akin to a “coarse graining” into the original MM graph, and constraints on where and how the input variable occurs. Other features of the graph, including the numerical values of parameters, can remain arbitrary, thereby explaining the formula’s ubiquity. For systems at thermodynamic equilibrium, we derive a necessary and sufficient condition. For systems away from thermodynamic equilibrium, especially those with irreversible reactions, distinct structural conditions arise and a general characterization remains open. Nevertheless, our results accommodate, in much greater generality, all examples known to us in the literature.


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