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    The transition state itself is defined as the dividing surface in phase space between reactants and products. It is generally assumed that all degrees of freedom are in thermodynamic equilibrium a sometimes problematic assumption.

    Enzymes Are Inherently Dynamical Entities. In this Account, we explore dynamics as a fundamental property of proteins and how it is related to enzymatic mechanism.

    It has long been recognized that a protein does not occupy a unique folded three-dimensional array of atoms, despite the impression that is common to almost all textbooks.

    This physical picture flows from the nature of the folded structure, whose stability and structural integrity is dictated by a large number of weak forces acting together.

    As such, enzymes are dynamic entities exhibiting distributions and fluctuations of catalytic rate constants, a notion termed dynamic disorder.

    It has been shown that an ensemble averaging of the single molecular results can yield Michaelis—Menten kinetics.

    However, the rate of catalysis for most enzymes depends on the rates of protein conformational changes. Given this, we need to ask whether the Michaelis complex, the enzyme—substrate construct that enters the Michaelis—Menten kinetic description of enzymatic catalysis, can be considered a single species.

    The most physically credible situation is that the Michaelis complex consists of an ensemble of conformations, each with its own effective k cat ; the single molecule experiments mentioned above provide strong evidence for this notion.

    Single molecule experiments have also demonstrated that when interconversion among the Michaelis conformations is slow compared with the chemical step, the system still exhibits Michaelis—Menten kinetics, but in this case the observed k cat is the weighted harmonic mean of k cat for all of the conformers depending on both the mean and distribution.

    From an experimental point of view, isolating that atomic motion of atoms associated with the chemical event against the vast background of motions is very hard indeed.

    Moreover, if part of the ensemble of the Michaelis complex is not very active by itself must convert to other substates that are active before chemistry can efficiently occur , this implies that the effective transition state energy of active conformations must be even correspondingly lower.

    It seems difficult enough to lower transition state energies to values permitting millisecond chemistry; why consider even lower values cf.

    Characterization of the Energy Landscape of Enzymes. It is difficult, both theoretically and experimentally, to determine the ensemble of substates that a folded protein adopts.

    For one thing, the number of states within the ensemble is huge. The issue at hand, to discern the functional relevance of the various substates, is even more demanding.

    One successful approach to picking out relevant conformations from the enormous background is to discern specific coordinates that are clearly associated with reactivity.

    For this purpose, vibrational spectroscopy has proved promising and very useful. When ligands bind to proteins, there are small but clear structural changes that show up in bond orders and concomitant changes to vibrational frequencies.

    For an enzyme—substrate complex, key bonds associated with the reaction coordinate are generally affected, and these become spectroscopic markers for catalytic propensity.

    For example, we determined a broad linear correlation of the bridging P—O R bond length in monosubstituted dianionic phosphates and the p K a of the substituent alcohol.

    Importantly, vibrational spectroscopy can discern these quite small changes in bond length. Hence, a vibrational analysis of this bond as the phosphate substrate binds to an enzyme and forms the Michaelis complex and its ensemble of structures is a monitor of functionally important substates.

    The bond itself can be specifically picked out from all other bonds within the Michaelis complex by employing isotope editing procedures.

    Since all vibrational modes not involving the isotope label subtract out, this procedure yields the spectrum of the enzyme bound phosphate modes. Our work has concentrated on the hydride transfer proteins, particularly lactate dehydrogenase LDH.

    Using isotope edited IR approaches, , 29 we have studied in detail the role of conformational heterogeneity and dynamics in the catalysis of hydride transfer by LDH.

    This enzyme catalyzes the reduction of pyruvate to lactate mediated by the transfer of a hydride from NADH to C-2 of pyruvate as shown in the cartoon of the active site Figure 1.

    High Resolution Image. Some key features to keep in mind to interpret these data are as follows. All the band profiles of Figure 2 are much broader so that the spectra represent a heterogeneous mixture of substates.

    The pyruvate molecule finds itself in varying hydrogen bonding environments, each with its own value for the stretch frequency.

    The important conclusion from all this is that the concentration of a specific conformation is proportional to the intensity of its IR band to a good approximation.

    The hydride transfer reaction between NADH and pyruvate in water proceeds very slowly. All this happens via a statistical search.

    Note, there is not a single conformation of molecules either in solution or when bound. Also note that the distribution is intermediate for pyruvate bound to the impaired LDH isozyme Figure 2 b.

    LDH enhances the rate of hydride transfer between NADH and pyruvate by about 10 14 M. A substantial portion of this rate enhancement is clearly a consequence of constraints imposed by the protein structure that bring about a restricted ensemble of more reactive conformational substates in the enzyme system.

    The Dynamics of the on-Enzyme Statistical Search for Reactivity. Protein structural fluctuations may be important both in the search for catalytically competent conformations and within such conformations, in the transition over the barrier that defines the chemical step.

    These structural dynamics span a wide range of times, from the femtosecond time scale of crossing the transition state to the millisecond time scale of overall enzyme turnover, or slower.

    Here we focus on the protein dynamics of the search for reactive conformations, expected to occur on the microsecond to millisecond time scale.

    Heterogeneity in the Michaelis state as described above for LDH may manifest in different ways in the observed enzyme turnover kinetics, depending on the relative time scale of the conformational dynamics.

    Heterogeneity in k cat is usually hidden in ensemble kinetics experiments because they only observe an average of the rate. In contrast, single molecule enzyme studies have demonstrated the existence of dynamic disorder in enzyme structure and its influence on k cat.

    Thus, an important question that remains is how protein conformational fluctuations change the rate of the chemical reaction.

    Recently it was shown that with LDH it is possible to resolve the heterogeneity in k cat due to conformational fluctuations of the Michaelis complex in ensemble experiments.

    These studies reveal how the dynamic disorder in the protein structure modulates the on-enzyme reactivity. Infrared spectroscopy was used to probe independently the differing reactivity of each Michaelis substate shown in Figure 2.

    The lower limit of this range is set by the response time of the instrument, and the upper limit is determined by the cooling time of the sample after the temperature-jump occurs typically several milliseconds for this sample configuration.

    The simplest model that fits the IR data is presented in Scheme 1 , which has multiple enzyme conformations at both the encounter and tightly bound complex stages of the reaction pathway.

    This model is also substantiated by significant previous work, which supports formation of a weakly binding encounter complex as the initial step, 19, 29, 36 protein structural fluctuations associated with forming the Michaelis complex, 21 and multiple conformations within the Michaelis state that do not directly interconvert, with one of these populations being incompetent toward conversion to lactate.

    Early on the reaction pathway, LDH forms an encounter complex with the pyruvate substrate, which then rearranges to the tightly bound states.

    This intermediate is obligatory, because there is no direct pathway between free substrate and the reactive conformations. The time scale of various protein structural rearrangements, including those that are somewhat slower than the chemistry step such as closure of the surface loop, residues 98—, that brings the key residue, Arg, into the active site; see Figure 1 , is similar to the time scale of the chemical step, such that they are strongly coupled kinetically.

    The different Michaelis substates do not directly interconvert, and most importantly, they exhibit different rates of conversion of pyruvate to lactate.

    Scheme 1. Best Fit Kinetic Scheme of the IR Transients in Figure 3. The key characteristic of the kinetics model in Scheme 1 is the emergence of branched pathways from the initial encounter complex, having Michaelis states of differing reactivity.

    The reactive states do not interconvert; therefore they are only populated through the initial encounter complex.

    This rate dependence is a consequence of the differing degree of polarization of the carbonyl bond for the different substates, as indicated by the stretch frequency.

    Therefore, these results directly correlate the heterogeneity in k cat with a specific structural feature of the Michaelis complex.

    Since these substates do not interconvert directly, the net flux through each depends on the branching from the initial encounter complex, and the overall turnover rate is a population weighted average of the multiple parallel pathways.

    Another important conclusion from this work is that the most reactive substate is not the most populated one. It is interesting to consider whether this incomplete optimization of the conformational search is a consequence of evolutionary fine-tuning driven by the requirements of homeostasis.

    The Nature of Dynamical Disorder Revealed for LDH. A kinetic picture of the flux through the enzyme emerges from this work, from the binding of substrate to the hunt though phase space to conformations that can undergo efficient chemistry, to the actual on-enzyme chemical event.

    For our system, the tightly bound conformations interconvert on the microsecond time scale, although the interconversion is not direct but rather through more loosely bound conformations.

    The search through conformation space on the nanosecond and slower times is very probably Markovian since the thermal fluctuations, occurring on the picosecond time scale, almost certainly disrupt any coherence in the system.

    That is, the system retains no or little memory of where it came in the interconversion from one substate to another. The dynamical fluctuating nature of the complex is quite directly revealed by the studies.

    The enzyme does not appear to be optimized to use the fastest pathway for on-enzyme chemistry preferentially but rather accesses multiple pathways in a search process that often selects slower ones.

    Consistent with these dynamics, the kinetic pathway can be separated into two parts: 1 the time it takes to form active conformations and the search time from less active to more active conformations and 2 the actual traversal from substrate to product.

    The first occurs on the nanosecond—microsecond time scale, while the latter occurs on the femtosecond time scale.

    Both the search process in the ground state through various reactive conformations and the chemical event are complicated, adopting multiple paths.

    It has a clear relationship to what is called intramolecular catalysis and effective concentration. For bimolecular reactions, such as that catalyzed by LDH, a rate enhancement of some 10 9 M can be realized from this effect.

    For LDH, it has been estimated that out of the 10 14 M rate enhancement brought about by LDH, some 10 6 M or more is due to intramolecular catalysis.

    Calculations of our collaborators suggest that the TS energy may well be very small, even just a few kilocalories per mole. This then places much of the overall free energy for the on-enzyme catalyzed reaction within the ground state.

    These findings are important for several reasons. One is that TST theory focuses on the energy barrier to the chemical event. It is very difficult to account for the dynamical nature of the ground state of the Michaelis complex by transition state concepts since dynamical disorder is not a starting feature of the theory.

    Taking dynamical disorder into account is typically not done or is rather ad hoc. Dynamical disorder may well play a larger or similar sized role in the measured Gibbs free energy of a reaction as the transition state energy associated with the chemical event.

    Often hyperthermophilic and psychrophilic enzymes employ the same basic structural architecture as their mesophilic counterparts leading to the idea that the transition state of the chemical reaction is largely the same for the three classes, at least for many enzymes.

    It is also widely believed that allosteric regulation of enzymes has to do with a modulation of the Michaelis complex ensemble population characteristics.

    These notions generally and quite particularly for LDH are quite thoroughly discussed in ref Author Contributions The manuscript was written through equal contributions of all authors.

    Funding Information This work supported by a grant from the National Institutes of Health General Medical Sciences, 5P01GM The authors declare no competing financial interest.

    Author Information. Brian Dyer - Department of Chemistry, Emory University, Atlanta, Georgia , United States. Brian Dyer. Science Washington, D.

    American Association for the Advancement of Science. A review and discussion, with 37 refs. Spontaneous hydrolysis of phosphodiester bonds, such as those present in the backbone of DNA, proceeds even more slowly at high temps.

    These values extend the known range of spontaneous rate consts. Values of the second-order rate const. The Depth of Chemical Time and Power of Enzymes as Catalysists Acc.

    Accounts of Chemical Research , 34 12 , CODEN: ACHRE4 ; ISSN: American Chemical Society. A review and discussion with 56 refs. The fastest known reactions include reactions catalyzed by enzymes, but the rate enhancements that enzymes produce have not been fully appreciated until recently.

    In the absence of enzymes, these same reactions are among the slowest that have ever been measured, some with half-times approaching the age of the Earth.

    This difference provides a measure of the proficiencies of enzymes as catalysts and their relative susceptibilities to inhibition by transition-state analog inhibitors.

    These comparisons also indicate a high level of synergism in the action of binding determinants of both the substrate and the enzyme, that are not directly involved in the chem.

    Ueber die Reaktionsgeschwindigkeit bei der Inversion von Rohrzucker durch Säuren Z. Etudes de Dynamiques Chimiques ; F. Muller and Co.

    Google Scholar There is no corresponding record for this reference. Physica The Hague , 7 , CODEN: PYSIA7 ; ISSN: A particle that is caught in a potential hole and that, through the shuttling action of Brownian motion, can escape over a potential barrier yields a suitable model for elucidating the applicability of the transition-state method for calcg.

    Reaction-Rate Therory: Fifty Years after Kramers Rev. Science Washington, DC, United States , , CODEN: SCIEAS ; ISSN: A review and discussion.

    Advances in transition state theory and computer simulations are providing new insights into the sources of enzyme catalysis. Both the lowering of the activation free energy and changes in the generalized transmission coeff.

    A framework for understanding these effects is presented, and the contributions of the different factors, as illustrated by specific enzymes, are identified and quantified by computer simulations.

    The resulting understanding of enzyme catalysis is used to comment on alternative proposals of how enzymes work. Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding ; Freeman and Co.

    Recent expts. The basis of the understanding is the observation that the energy landscape is complex: proteins can assume a large no. The concepts that emerge from studies of the conformational substates and the motions between them permit a quant.

    Flucting Enzymes: Lessions from Single-Molecule Studies Acc. Min, Wei; English, Brian P. Accounts of Chemical Research , 38 12 , CODEN: ACHRE4 ; ISSN: A review.

    Recent single-mol. The rate const. The authors discuss the unique information extractable from these expts.

    A theor. When Does the Michaelis-Menton Equation Hold for Fluctuating Wnzymes? Min, Wei; Gopich, Irina V. Sunney; Szabo, Attila.

    Journal of Physical Chemistry B , 41 , CODEN: JPCBFK ; ISSN: Enzymes are dynamic entities since both their conformation and catalytic activity fluctuate over time.

    When such fluctuations are relatively fast, it is not surprising that the classical Michaelis-Menten MM relation between the steady-state enzymic velocity and the substrate concn.

    However, recent single-mol. The purpose of this paper was to examine various scenarios in which slowly fluctuating enzymes would still obey the MM relation.

    Specifically, the authors considered: 1 the quasi-static condition e. For each of these scenarios, the phys. Finally, as an example, the theor.

    Iversen, Lars; Tu, Hsiung-Lin; Lin, Wan-Chen; Christensen, Sune M. The activation of small GTPase H-Ras by guanine nucleotide exchange factor, son of sevenless SOS , is an important hub for signal transduction.

    Multiple layers of regulation, through protein and membrane interactions, govern the activity of SOS. Here, the authors characterized the specific activity of individual SOS mols.

    The expected allosteric activation of SOS by Ras-GTP was conspicuously absent in the mean rate. However, fluctuations into highly active states were modulated by Ras-GTP.

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