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Title: Biochemistry of Dissimilatory Sulfur Oxidation

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.

Authors:
Publication Date:
Research Org.:
Xavier University, New Orleans, LA (US)
Sponsoring Org.:
USDOE Office of Energy Research (ER) (US)
OSTI Identifier:
836587
DOE Contract Number:  
FG02-94ER20156
Resource Type:
Technical Report
Resource Relation:
Other Information: PBD: 30 May 2003
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; ADENOSINE; ADHESION; BACTERIA; BIOCHEMISTRY; ELECTRONS; ENERGY CONSERVATION; ENZYMES; FUNCTIONALS; IMPEDANCE; LIGHT SCATTERING; OXIDASES; OXIDATION; OXIDOREDUCTASES; SUBSTRATES; SULFUR

Citation Formats

Blake II, R. Biochemistry of Dissimilatory Sulfur Oxidation. United States: N. p., 2003. Web. doi:10.2172/836587.
Blake II, R. Biochemistry of Dissimilatory Sulfur Oxidation. United States. doi:10.2172/836587.
Blake II, R. Fri . "Biochemistry of Dissimilatory Sulfur Oxidation". United States. doi:10.2172/836587. https://www.osti.gov/servlets/purl/836587.
@article{osti_836587,
title = {Biochemistry of Dissimilatory Sulfur Oxidation},
author = {Blake II, R.},
abstractNote = {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.},
doi = {10.2172/836587},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Fri May 30 00:00:00 EDT 2003},
month = {Fri May 30 00:00:00 EDT 2003}
}

Technical Report:

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