Literature DB >> 23318152

Why nature really chose phosphate.

Shina C L Kamerlin1, Pankaz K Sharma, Ram B Prasad, Arieh Warshel.   

Abstract

Phosphoryl transfer plays key roles in signaling, energy transduction, protein synthesis, and maintaining the integrity of the genetic material. On the surface, it would appear to be a simple nucleophile displacement reaction. However, this simplicity is deceptive, as, even in aqueous solution, the low-lying d-orbitals on the phosphorus atom allow for eight distinct mechanistic possibilities, before even introducing the complexities of the enzyme catalyzed reactions. To further complicate matters, while powerful, traditional experimental techniques such as the use of linear free-energy relationships (LFER) or measuring isotope effects cannot make unique distinctions between different potential mechanisms. A quarter of a century has passed since Westheimer wrote his seminal review, 'Why Nature Chose Phosphate' (Science 235 (1987), 1173), and a lot has changed in the field since then. The present review revisits this biologically crucial issue, exploring both relevant enzymatic systems as well as the corresponding chemistry in aqueous solution, and demonstrating that the only way key questions in this field are likely to be resolved is through careful theoretical studies (which of course should be able to reproduce all relevant experimental data). Finally, we demonstrate that the reason that nature really chose phosphate is due to interplay between two counteracting effects: on the one hand, phosphates are negatively charged and the resulting charge-charge repulsion with the attacking nucleophile contributes to the very high barrier for hydrolysis, making phosphate esters among the most inert compounds known. However, biology is not only about reducing the barrier to unfavorable chemical reactions. That is, the same charge-charge repulsion that makes phosphate ester hydrolysis so unfavorable also makes it possible to regulate, by exploiting the electrostatics. This means that phosphate ester hydrolysis can not only be turned on, but also be turned off, by fine tuning the electrostatic environment and the present review demonstrates numerous examples where this is the case. Without this capacity for regulation, it would be impossible to have for instance a signaling or metabolic cascade, where the action of each participant is determined by the fine-tuned activity of the previous piece in the production line. This makes phosphate esters the ideal compounds to facilitate life as we know it.

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Year:  2013        PMID: 23318152      PMCID: PMC7032660          DOI: 10.1017/S0033583512000157

Source DB:  PubMed          Journal:  Q Rev Biophys        ISSN: 0033-5835            Impact factor:   5.318


  375 in total

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Authors:  A Warshel; J K Hwang; J Aqvist
Journal:  Faraday Discuss       Date:  1992       Impact factor: 4.008

Review 2.  Mechanisms of signaling and related enzymes.

Authors:  A S Mildvan
Journal:  Proteins       Date:  1997-12

3.  Conformation and hydrogen ion titration of proteins: a continuum electrostatic model with conformational flexibility.

Authors:  T J You; D Bashford
Journal:  Biophys J       Date:  1995-11       Impact factor: 4.033

4.  Mutagenesis of three residues, isoleucine-60, threonine-61, and aspartic acid-80, implicated in the GTPase activity of Escherichia coli elongation factor Tu.

Authors:  I M Krab; A Parmeggiani
Journal:  Biochemistry       Date:  1999-10-05       Impact factor: 3.162

5.  How conformational dynamics of DNA polymerase select correct substrates: experiments and simulations.

Authors:  Serdal Kirmizialtin; Virginia Nguyen; Kenneth A Johnson; Ron Elber
Journal:  Structure       Date:  2012-04-03       Impact factor: 5.006

Review 6.  Protein tyrosine phosphatase 1B inhibitors for diabetes.

Authors:  Theodore O Johnson; Jacques Ermolieff; Michael R Jirousek
Journal:  Nat Rev Drug Discov       Date:  2002-09       Impact factor: 84.694

7.  The catalytic effect of dihydrofolate reductase and its mutants is determined by reorganization energies.

Authors:  Hanbin Liu; Arieh Warshel
Journal:  Biochemistry       Date:  2007-05-01       Impact factor: 3.162

8.  Substitution of histidine-84 and the GTPase mechanism of elongation factor Tu.

Authors:  R H Cool; A Parmeggiani
Journal:  Biochemistry       Date:  1991-01-15       Impact factor: 3.162

9.  Computational study of the phosphoryl transfer catalyzed by a cyclin-dependent kinase.

Authors:  Marco De Vivo; Andrea Cavalli; Paolo Carloni; Maurizio Recanatini
Journal:  Chemistry       Date:  2007       Impact factor: 5.236

10.  A Trojan horse transition state analogue generated by MgF3- formation in an enzyme active site.

Authors:  Nicola J Baxter; Luis F Olguin; Marko Golicnik; Guoqiang Feng; Andrea M Hounslow; Wolfgang Bermel; G Michael Blackburn; Florian Hollfelder; Jonathan P Waltho; Nicholas H Williams
Journal:  Proc Natl Acad Sci U S A       Date:  2006-09-21       Impact factor: 11.205

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  80 in total

1.  Enhancing Paradynamics for QM/MM Sampling of Enzymatic Reactions.

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Review 2.  Imaging Adenosine Triphosphate (ATP).

Authors:  Megha Rajendran; Eric Dane; Jason Conley; Mathew Tantama
Journal:  Biol Bull       Date:  2016-08       Impact factor: 1.818

3.  Multiscale modeling of biological functions: from enzymes to molecular machines (Nobel Lecture).

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Journal:  Angew Chem Int Ed Engl       Date:  2014-07-24       Impact factor: 15.336

4.  Modular Synthesis of Novel Macrocycles Bearing α,β-Unsaturated Chemotypes through a Series of One-Pot, Sequential Protocols.

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Journal:  Chemistry       Date:  2016-04-05       Impact factor: 5.236

5.  Explore the reaction mechanism of the Maillard reaction: a density functional theory study.

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Journal:  J Mol Model       Date:  2015-05-02       Impact factor: 1.810

6.  Single-molecule electrometry.

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Journal:  Nat Nanotechnol       Date:  2017-03-13       Impact factor: 39.213

Review 7.  Control of rotation of the F1FO-ATP synthase nanomotor by an inhibitory α-helix from unfolded ε or intrinsically disordered ζ and IF1 proteins.

Authors:  Francisco Mendoza-Hoffmann; Mariel Zarco-Zavala; Raquel Ortega; José J García-Trejo
Journal:  J Bioenerg Biomembr       Date:  2018-09-28       Impact factor: 2.945

8.  Quantitative exploration of the molecular origin of the activation of GTPase.

Authors:  Ram Prasad B; Nikolay V Plotnikov; Jeronimo Lameira; Arieh Warshel
Journal:  Proc Natl Acad Sci U S A       Date:  2013-11-26       Impact factor: 11.205

9.  Empirical valence bond simulations of the chemical mechanism of ATP to cAMP conversion by anthrax edema factor.

Authors:  Letif Mones; Wei-Jen Tang; Jan Florián
Journal:  Biochemistry       Date:  2013-04-02       Impact factor: 3.162

Review 10.  Invited review: Small GTPases and their GAPs.

Authors:  Ashwini K Mishra; David G Lambright
Journal:  Biopolymers       Date:  2016-08       Impact factor: 2.505

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