Biochemistry of Dissimilatory Sulfur Oxidation

Blake II, R.

Xavier University, New Orleans, LA (United States)

关键词: Light Scattering;    Oxidation;    Oxidoreductases;    Enzymes;    Biochemistry;   

DOI  :  10.2172/836587
RP-ID  :  NONE
RP-ID  :  FG02-94ER20156
RP-ID  :  836587

美国|英语

来源: UNT Digital Library

【 摘 要 】

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.