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Biochemistry of Dissimilatory Sulfur Oxidation. Final Technical Report.

DE2005836587

Publication Date	2003
Personal Author	Blake, R.
Page Count	14
Abstract	The long term goals of this research were to define the substrate oxidation pathways, the electron transport mechanisms, and the modes of energy conservation employed during the dissimilatory oxidation of sulfur practiced by various species of the thiobacilli. Specific adhesion of the thiobacilli to elemental sulfur was studied by electrical impedance, dynamic light scattering, laser Doppler velocimetry, and optical trapping methods. The conclusion is that the thiobacilli appear to express specific receptors that enable the bacteria to recognize and adhere to insoluble sulfur. The enzyme tetrathionate oxidase was purified from two species of the thiobacilli. Extensive structural and functional studies were conducted on adenosine 5'-phosphosulfate reductase purified from cell-free extracts of Thiobacillus denitrificans. The kinetic mechanism of rhodanese was studied.
Keywords	Sulfur-oxidizing bacteria Antibodies Bacillus Desulfurization Enzyme activity Oxidation Progress report Electrical impedance Thiobacilli
Source Agency	Technical Information Center Oak Ridge Tennessee
Corporate Authors	Xavier Univ. of Louisiana, New Orleans.; Department of Energy, Washington, DC.
Supplemental Notes	Sponsored by Department of Energy, Washington, DC.
Document Type	Technical Report
NTIS Issue Number	200520

Biochemistry of Dissimilatory Sulfur Oxidation. Final Technical Report.

Biochemistry of Dissimilatory Sulfur Oxidation. Final Technical Report.
DE2005836587

Publication Date	2003
Personal Author	Blake, R.
Page Count	14
Abstract	The long term goals of this research were to define the substrate oxidation pathways, the electron transport mechanisms, and the modes of energy conservation employed during the dissimilatory oxidation of sulfur practiced by various species of the thiobacilli. Specific adhesion of the thiobacilli to elemental sulfur was studied by electrical impedance, dynamic light scattering, laser Doppler velocimetry, and optical trapping methods. The conclusion is that the thiobacilli appear to express specific receptors that enable the bacteria to recognize and adhere to insoluble sulfur. The enzyme tetrathionate oxidase was purified from two species of the thiobacilli. Extensive structural and functional studies were conducted on adenosine 5'-phosphosulfate reductase purified from cell-free extracts of Thiobacillus denitrificans. The kinetic mechanism of rhodanese was studied.
Keywords	Sulfur-oxidizing bacteria Antibodies Bacillus Desulfurization Enzyme activity Oxidation Progress report Electrical impedance Thiobacilli
Source Agency	Technical Information Center Oak Ridge Tennessee
Corporate Authors	Xavier Univ. of Louisiana, New Orleans.; Department of Energy, Washington, DC.
Supplemental Notes	Sponsored by Department of Energy, Washington, DC.
Document Type	Technical Report
NTIS Issue Number	200520