Search arXivSearch

arXiv · 1412.3196

Single-enzyme kinetics with branched pathways: exact theory and series expansion

Abstract

The progress of the successive rounds of catalytic conversion of substrates into product(s) by a single enzyme is characterized by the distribution of turnover times. Establishing the most general form of dependence of this distribution on the substrate concentration [S] is one of the fundamental challenges in single molecule enzymology. The distribution of the times of dwell of a molecular motor at the successive positions on its track is an analogous quantity. We derive approximate series expansions for the [ATP]-dependence of the first two moments of the dwell time distributions of motors that catalyze hydrolysis of ATP to draw input energy. Comparison between our results for motors with branched pathways and the corresponding expressions reported earlier for linear enzymatic pathways provides deep insight into the effects of the branches. Such insight is likely to help in discovering the most general form of [S]-dependence of these fundamental distributions.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Ashok Garai, Debashish Chowdhury. 2014-12-10. Single-enzyme kinetics with branched pathways: exact theory and series expansion. https://arxiv.org/abs/1412.3196

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related papers

Intrinsic Matching Frustration in Fluctuating Finite Systems

We formulate intrinsic matching frustration (IMF), a fluctuation-induced, kinetics-independent reduction in the mean capacity permitted by a prescribed matching rule. For complementary one-to-one matching, the instantaneous capacity is set by the minority population, so fluctuations produce a nonzero mean deficit even when the two populations are balanced on average. At finite size, this deficit depends on the full distribution of the population difference and is determined by its variance alone only in the Gaussian limit. Compartmentalization hides matching capacity by preventing cancellation between local imbalances of opposite sign. Fusion releases this hidden capacity monotonically under coarse graining, producing a measurable recovery of product yield following local reaction to completion.

physics.chem-ph

Phonon chirality as an additive control of CISS: a symmetry-protected law

Chirality-induced spin selectivity (CISS) is usually associated with molecular handedness. The possible contribution of chiral phonons is less established. We study a helical tight-binding model in which local phonon angular momentum modulates spin-dependent nearest-neighbor hopping. Fewest-switches surface hopping calculations give the transmitted spin polarization $\mathrm{SP}=aC+b\mathrm{PH}$. Here $C$ is the molecular chirality and $\mathrm{PH}$ is the phonon chirality. A mirror symmetry reverses $C$, $\mathrm{PH}$, and $\mathrm{SP}$ simultaneously. This symmetry excludes both a chirality-independent offset and a $C\cdot\mathrm{PH}$ term. The phonon contribution can therefore enhance, cancel, or reverse the molecular CISS signal.

physics.chem-ph

A fast physics-based matrix model for the impedance of a PEM fuel cell: Incorporating functionally graded catalyst layer and channel impedances

We extend a recent physics-based matrix model for calculating PEM fuel cell impedance (doi:10.1149/2754-2734/ad6ce8) to cases of low air flow stoichiometry and functionally graded cathode catalyst layers (CCLs). We demonstrate that the matrix model produces accurate spectra and is almost three orders of magnitude faster than a model based on the standard boundary-value problem solver. The physics-based matrix model can compete with equivalent circuit models for fitting experimental EIS spectra, particularly those measured from cells with functionally graded CCL.

physics.chem-ph