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- Title
- INVESTIGATION OF VISUAL REQUIREMENTS FOR CHANGE DETECTION.
- Creator
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Niederman, Elisabeth, Hancock, Peter, University of Central Florida
- Abstract / Description
-
In this study, participants performed a change detection task. Specifically we examined whether participants had to fixate on a difference between two images before they could detect it. Thirty-six participants performed a change detection task in either a 3 minute or a 1.5 minute condition. We found a significant interaction between task duration and fixation type (whether the participant had fixated on the difference in both, one, or neither image). Participants found a greater number of...
Show moreIn this study, participants performed a change detection task. Specifically we examined whether participants had to fixate on a difference between two images before they could detect it. Thirty-six participants performed a change detection task in either a 3 minute or a 1.5 minute condition. We found a significant interaction between task duration and fixation type (whether the participant had fixated on the difference in both, one, or neither image). Participants found a greater number of differences given more time only when they fixated on the difference in both images. The number of differences which were detected by participants with a fixation on only one image or on neither image did not increase with a corresponding increase in time, indicating that some mechanical error may be involved. This suggests that participants need to fixate on a difference before being able to detect it.
Show less - Date Issued
- 2013
- Identifier
- CFH0004500, ucf:45152
- Format
- Document (PDF)
- PURL
- http://purl.flvc.org/ucf/fd/CFH0004500
- Title
- Biochemical Characterization of the NifB Enzyme and NifB-cofactor.
- Creator
-
Gevorkyan, Jirair, Igarashi, Robert, Belfield, Kevin, Hernandez, Florencio, Kuebler, Stephen, Vonkalm, Laurence, University of Central Florida
- Abstract / Description
-
The Mo-nitrogenase complex is composed of two components, Fe-protein and MoFe-protein. This complex is able to catalyze the reduction of N2 through the MgATP dependent transfer of electrons from the Fe-protein Fe4S4 cluster to the MoFe-protein P-cluster and, subsequently, to the iron-molybdenum cofactor (FeMo-co). FeMo-co is a Fe7S9MoC-(R)-homocitrate cluster and has two biosynthetic precursors, NifB-co and L-cluster, of unknown structure and composition. The biosynthesis of FeMo-co is an...
Show moreThe Mo-nitrogenase complex is composed of two components, Fe-protein and MoFe-protein. This complex is able to catalyze the reduction of N2 through the MgATP dependent transfer of electrons from the Fe-protein Fe4S4 cluster to the MoFe-protein P-cluster and, subsequently, to the iron-molybdenum cofactor (FeMo-co). FeMo-co is a Fe7S9MoC-(R)-homocitrate cluster and has two biosynthetic precursors, NifB-co and L-cluster, of unknown structure and composition. The biosynthesis of FeMo-co is an enigmatic process that minimally requires NifB, NifEN, Fe-protein, MoO42-, (R)-homocitrate and S-adenolsylmethionine.A means to isolate the NifB enzyme for characterization has been developed through use of a GST-fusion tag. Double recombination of A. vinelandii strains with a constructed vector has yielded strains capable of nif promoter regulated expression of GST-NifB. Extracts of strains containing GST-NifB were shown to activate the Mo-nitrogenase complex in biochemical complementation assays. Mass spectroscopy was then used to verify successful isolation of GST-NifB by GSH-Sepharose affinity purification.The number of NifB-co ligand binding sites and ligand types were examined by EXAFS analysis of samples containing selenol and thiol ligands. A Fe6S9C model for NifB-co was optimized to best fit the EXAFS data, where a 2-fold discrepancy in binding sites implied by thiol or selenol only ligand samples suggests Fe-(?2S)-Fe binding in the absence of Se. Samples containing heterogeneous ligand types indicated that NifX bound NifB-co ligates to four cysteine residues and one molecule of DTT.
Show less - Date Issued
- 2013
- Identifier
- CFE0004682, ucf:49865
- Format
- Document (PDF)
- PURL
- http://purl.flvc.org/ucf/fd/CFE0004682
