scholarly journals Determination of the Distance between the Mo(V) and Fe(III) Heme Centers of Wild Type Human Sulfite Oxidase by Pulsed EPR Spectroscopy

2012 ◽  
Vol 116 (6) ◽  
pp. 1942-1950 ◽  
Author(s):  
Andrei V. Astashkin ◽  
Asha Rajapakshe ◽  
Matthew J. Cornelison ◽  
Kayunta Johnson-Winters ◽  
John H. Enemark
Keyword(s):  
Epr Spectroscopy ◽  
Sulfite Oxidase ◽  
Wild Type ◽  
Pulsed Epr ◽  
Human Sulfite Oxidase

scholarly journals Structural Studies of the Molybdenum Center of the Pathogenic R160Q Mutant of Human Sulfite Oxidase by Pulsed EPR Spectroscopy and17O and33S Labeling

2008 ◽  
Vol 130 (26) ◽  
pp. 8471-8480 ◽  
Author(s):  
Andrei V. Astashkin ◽  
Kayunta Johnson-Winters ◽  
Eric L. Klein ◽  
Changjian Feng ◽  
Heather L. Wilson ◽  
...  
Keyword(s):  
Epr Spectroscopy ◽  
Sulfite Oxidase ◽  
Structural Studies ◽  
Pulsed Epr ◽  
Human Sulfite Oxidase

scholarly journals Studies of the Mo(V) center of the Y343F mutant of human sulfite oxidase by variable frequency pulsed EPR spectroscopy

2008 ◽  
Vol 361 (4) ◽  
pp. 941-946 ◽  
Author(s):  
Arnold M. Raitsimring ◽  
Andrei V. Astashkin ◽  
Changjian Feng ◽  
Heather L. Wilson ◽  
K.V. Rajagopalan ◽  
...  
Keyword(s):  
Epr Spectroscopy ◽  
Sulfite Oxidase ◽  
Variable Frequency ◽  
Pulsed Epr ◽  
Human Sulfite Oxidase

scholarly journals Consensus structures of the Mo(v) sites of sulfite-oxidizing enzymes derived from variable frequency pulsed EPR spectroscopy, isotopic labelling and DFT calculations

2017 ◽  
Vol 46 (39) ◽  
pp. 13202-13210 ◽  
Author(s):  
John H. Enemark
Keyword(s):  
Dft Calculations ◽  
Epr Spectroscopy ◽  
Sulfite Oxidase ◽  
Variable Frequency ◽  
Isotopic Labelling ◽  
Pulsed Epr

The “blocked” form of sulfite oxidase has O-bound sulfite, and only the coordinated and remote O atoms exchange with H217O.

Structures of the Mo(V) Forms of Sulfite Oxidase fromArabidopsis thalianaby Pulsed EPR Spectroscopy†

Biochemistry ◽  
2005 ◽  
Vol 44 (40) ◽  
pp. 13274-13281 ◽  
Author(s):  
Andrei V. Astashkin ◽  
Brian L. Hood ◽  
Changjian Feng ◽  
Russ Hille ◽  
Ralf R. Mendel ◽  
...  
Keyword(s):  
Epr Spectroscopy ◽  
Sulfite Oxidase ◽  
Pulsed Epr

scholarly journals Determination of the distance between Yox⋅ Z and Q−⋅ A in photosystem II by pulsed EPR spectroscopy on light-induced radical pairs

FEBS Letters ◽  
1999 ◽  
Vol 442 (1) ◽  
pp. 79-82 ◽  
Author(s):  
Stephan G. Zech ◽  
Jens Kurreck ◽  
Gernot Renger ◽  
Wolfgang Lubitz ◽  
Robert Bittl
Keyword(s):  
Photosystem Ii ◽  
Epr Spectroscopy ◽  
Radical Pairs ◽  
Pulsed Epr

scholarly journals Structures and reaction pathways of the molybdenum centres of sulfite-oxidizing enzymes by pulsed EPR spectroscopy

2008 ◽  
Vol 36 (6) ◽  
pp. 1129-1133 ◽  
Author(s):  
John H. Enemark ◽  
Andrei V. Astashkin ◽  
Arnold M. Raitsimring
Keyword(s):  
Epr Spectroscopy ◽  
Reaction Pathways ◽  
Oxidase Deficiency ◽  
Pulsed Epr ◽  
Product Release ◽  
Nuclear Quadrupole Interactions ◽  
Sulfite Oxidase Deficiency ◽  
Nuclear Quadrupole ◽  
Human Sulfite Oxidase ◽  
Insight Into

SOEs (sulfite-oxidizing enzymes) are physiologically vital and occur in all forms of life. During the catalytic cycle, the five-co-ordinate square pyramidal oxo-molybdenum active site passes through the Mo(V) state, and intimate details of the structure can be obtained from variable frequency pulsed EPR spectroscopy through the hyperfine and nuclear quadrupole interactions of nearby magnetic nuclei. By employing variable spectrometer operational frequencies, it is possible to optimize the measurement conditions for difficult quadrupolar nuclei of interest (e.g. 17O, 33S, 35Cl and 37Cl) and to simplify the interpretation of the spectra. Isotopically labelled model Mo(V) compounds provide further insight into the electronic and geometric structures and chemical reactions of the enzymes. Recently, blocked forms of SOEs having co-ordinated sulfate, the reaction product, were detected using 33S (I=3/2) labelling. This blocking of product release is a possible contributor to fatal human sulfite oxidase deficiency in young children.

scholarly journals Evaluation of wild-type MIC distributions as a tool for determination of clinical breakpoints for Mycobacterium tuberculosis

2009 ◽  
Vol 64 (4) ◽  
pp. 786-793 ◽  
Author(s):  
T. Schon ◽  
P. Jureen ◽  
C. G. Giske ◽  
E. Chryssanthou ◽  
E. Sturegard ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Wild Type ◽  
Clinical Breakpoints

scholarly journals Expression Level of Mature miR172 in Wild Type and StSUT4-Silenced Plants of Solanum tuberosum Is Sucrose-Dependent

2021 ◽  
Vol 22 (3) ◽  
pp. 1455
Author(s):  
Varsha Garg ◽  
Aleksandra Hackel ◽  
Christina Kühn
Keyword(s):  
Solanum Tuberosum ◽  
Wild Type ◽  
Potato Plants ◽  
Mature Leaves ◽  
In Vitro Plantlets ◽  
Long Time ◽  
Short Time ◽  
Cut Leaves

In potato plants, the phloem-mobile miR172 is involved in the sugar-dependent transmission of flower and tuber inducing signal transduction pathways and a clear link between solute transport and the induction of flowering and tuberization was demonstrated. The sucrose transporter StSUT4 seems to play an important role in the photoperiod-dependent triggering of both developmental processes, flowering and tuberization, and the phenotype of StSUT4-inhibited potato plants is reminiscent to miR172 overexpressing plants. The first aim of this study was the determination of the level of miR172 in sink and source leaves of StSUT4-silenced as well as StSUT4-overexpressing plants in comparison to Solanum tuberosum ssp. Andigena wild type plants. The second aim was to investigate the effect of sugars on the level of miRNA172 in whole cut leaves, as well as in whole in vitro plantlets that were supplemented with exogenous sugars. Experiments clearly show a sucrose-dependent induction of the level of mature miR172 in short time as well as long time experiments. A sucrose-dependent accumulation of miR172 was also measured in mature leaves of StSUT4-silenced plants where sucrose export is delayed and sucrose accumulates at the end of the light period.

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