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Flare-productive active regions.

ABSTRACT: Strong solar flares and coronal mass ejections, here defined not only as the bursts of electromagnetic radiation but as the entire process in which magnetic energy is released through magnetic reconnection and plasma instability, emanate from active regions (ARs) in which high magnetic non-potentiality resides in a wide variety of forms. This review focuses on the formation and evolution of flare-productive ARs from both observational and theoretical points of view. Starting from a general introduction of the genesis of ARs and solar flares, we give an overview of the key observational features during the long-term evolution in the pre-flare state, the rapid changes in the magnetic field associated with the flare occurrence, and the physical mechanisms behind these phenomena. Our picture of flare-productive ARs is summarized as follows: subject to the turbulent convection, the rising magnetic flux in the interior deforms into a complex structure and gains high non-potentiality; as the flux appears on the surface, an AR with large free magnetic energy and helicity is built, which is represented by ? -sunspots, sheared polarity inversion lines, magnetic flux ropes, etc; the flare occurs when sufficient magnetic energy has accumulated, and the drastic coronal evolution affects magnetic fields even in the photosphere. We show that the improvement of observational instruments and modeling capabilities has significantly advanced our understanding in the last decades. Finally, we discuss the outstanding issues and future perspective and further broaden our scope to the possible applications of our knowledge to space-weather forecasting, extreme events in history, and corresponding stellar activities.

SUBMITTER: Toriumi S

PROVIDER: S-EPMC6530820 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

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Flare-productive active regions.

Toriumi Shin S Wang Haimin H

Living reviews in solar physics 20190521 1

Strong solar flares and coronal mass ejections, here defined not only as the bursts of electromagnetic radiation but as the entire process in which magnetic energy is released through magnetic reconnection and plasma instability, emanate from active regions (ARs) in which high magnetic non-potentiality resides in a wide variety of forms. This review focuses on the formation and evolution of flare-productive ARs from both observational and theoretical points of view. Starting from a general intro ...[more]

PMID: 31178676

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Project description:The in vitro evolution and engineering of quorum-quenching lactonases with enhanced reactivities was achieved using a thermostable GKL enzyme as a template, yielding the E101G/R230C GKL mutant with increased catalytic activity and a broadened substrate range [Chow, J. Y., Xue, B., Lee, K. H., Tung, A., Wu, L., Robinson, R. C., and Yew, W. S. (2010) J. Biol. Chem. 285, 40911-40920]. This enzyme possesses the (?/?)8-barrel fold and is a member of the PLL (phosphotriesterase-like lactonase) group of enzymes within the amidohydrolase superfamily that hydrolyze N-acyl-homoserine lactones, which mediate the quorum-sensing pathways of bacteria. The structure of the evolved N-butyryl-l-homoserine lactone (substrate)-bound E101G/R230C GKL enzyme was determined, in the presence of the inactivating D266N mutation, to a resolution of 2.2 Å to provide an explanation for the observed rate enhancements. In addition, the substrate-bound structure of the catalytically inactive E101N/D266N mutant of the manganese-reconstituted enzyme was determined to a resolution of 2.1 Å and the structure of the ligand-free, manganese-reconstituted E101N mutant to a resolution of 2.6 Å, and the structures of ligand-free zinc-reconstituted wild-type, E101N, R230D, and E101G/R230C mutants of GKL were determined to resolutions of 2.1, 2.1, 1.9, and 2.0 Å, respectively. In particular, the structure of the evolved E101G/R230C mutant of GKL provides evidence of a catalytically productive active site architecture that contributes to the observed enhancement of catalysis. At high concentrations, wild-type and mutant GKL enzymes are differentially colored, with absorbance maxima in the range of 512-553 nm. The structures of the wild-type and mutant GKL provide a tractable link between the origins of the coloration and the charge-transfer complex between the ?-cation and Tyr99 within the enzyme active site. Taken together, this study provides evidence of the modulability of enzymatic catalysis through subtle changes in enzyme active site architecture.

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Flare-productive active regions.

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Flare-productive active regions.

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