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IGI Global eBooks

Logistic vs. W-Lambert Information in Modeling Enzyme Kinetics at Quantum Level

Mihai V. Putz, Ana-Maria Putz

Published Feb 26, 2014• 0 citations
Publisher

Abstract

The logistic temporal solution of the generalized Michaelis-Menten kinetics is employed to provide a quantum basis for the tunneling time and energy evaluations of Brownian enzymic reactions. The mono-substrate and mixed inhibition cases are treated and the associated quantum diagrams of the reaction mechanisms are depicted in terms of intermediate enzyme complexes. The methodology is suited for practically controlling of the enzymic activity throughout absorption spectroscopy.

DOI
10.4018/978-1-4666-5125-8.ch066

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The logistic temporal solution of the generalized Michaelis-Menten kinetics is employed to provide a quantum basis for the tunneling time and energy evaluations of Brownian enzymic reactions. The mono-substrate and mixed inhibition cases are treated and the associated quantum diagrams of the reaction mechanisms are depicted in terms of intermediate enzyme complexes. The methodology is suited for practically controlling of the enzymic activity throughout absorption spectroscopy.
In this introductory paper we overview existing approaches to enzyme – catalysed reactions. From the Michaelis – Menten kinetics to quantum scatterings several models are considered. We try to introduce our ”information – driven measurement engines” (an other model of enzyme action) in relation to existent theories. We conclude that our approach is a special type of quantum mechanical treatment of enzyme catalysed reactions, in its nascent form. It is, we suppose, stands more in relation to a hypothetical gas – phase scattering, maybe even resonance scattering, as a one – dimensional vacuum energy – dependent motion along the reaction path. We are aware that at this time, no realistic gas – phase scattering is available in the area, and our approach is thus similarly hypothetical. Still, it might provide a fresh view on enzyme – catalysed reactions, utilising a somewhat unusual Hamiltonian second – order tensor operator formalism. During arriving at our goal, we give some more extensive review devoted to current catalyzed and uncatalized reaction investigations, of a pure chemical and biochemical nature, exploring both experimental and theoretical procedures.
In this introductory paper we overview existing approaches to enzyme – catalysed reactions. From the Michaelis – Menten kinetics to quantum scatterings several models are considered. We try to introduce our ”information – d riven measurement engines” (an other model of enzyme action) in relation to existent theories. We conclude that our approach is a special type of quantum mechanical treatment of enzyme catalysed reactions, in its nascent form. It is, we suppose, stands mor e in relation to a hypothetical gas – phase scattering, maybe even resonance scattering, as a one – dimensional vacuum energy – dependent motion along the reaction path. We are aware that at this time, no realistic gas – phase scattering is available in th e area, and our approach is thus similarly hypothetical. Still, it might provide a fresh view on enzyme – catalysed reactions, utilising a somewhat unusual Hamiltonian second – order tensor operator formalism. During arriving at our goal, we give some mor e extensive review devoted to current cataly s ed and uncatal y s ed reaction investigations, of a pure chemical and biochemical nature, exploring both experimental and theoretical procedures.
Separating the dynamics of variables that evolve on different timescales is a common assumption in exploring complex systems, and a great deal of progress has been made in understanding chemical systems by treating independently the fast processes of an activated chemical species from the slower processes that proceed activation. Protein motion underlies all biocatalytic reactions, and understanding the nature of this motion is central to understanding how enzymes catalyze reactions with such specificity and such rate enhancement. This understanding is challenged by evidence of breakdowns in the separability of timescales of dynamics in the active site form motions of the solvating protein. Quantum simulation methods that bridge these timescales by simultaneously evolving quantum and classical degrees of freedom provide an important method on which to explore this breakdown. In the following dissertation, three problems of enzyme catalysis are explored through quantum simulation.