Arsenite oxidation by the heterotroph Hydrogenophaga sp. str. NT-14: the arsenite oxidase and its physiological electron acceptor
Autor: | Joanne M. Santini, Rachel N. vanden Hoven |
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Rok vydání: | 2004 |
Předmět: |
Cytochrome
Protein Conformation Iron Molecular Sequence Data Biophysics Heterotroph Biochemistry Cofactor Comamonadaceae chemistry.chemical_compound Sequence Analysis Protein Amino Acid Sequence Arsenite Molybdenum chemistry.chemical_classification Arsenite oxidase Alcaligenes faecalis Sequence Homology Amino Acid Molecular mass biology Electron transport Cytochromes c Cell Biology Electron acceptor biology.organism_classification Electron transport chain Molecular Weight Oxygen Protein Subunits chemistry biology.protein Electrophoresis Polyacrylamide Gel Oxidoreductases Oxidation-Reduction |
Zdroj: | Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1656:148-155 |
ISSN: | 0005-2728 |
DOI: | 10.1016/j.bbabio.2004.03.001 |
Popis: | Heterotrophic arsenite oxidation by Hydrogenophaga sp. str. NT-14 is coupled to the reduction of oxygen and appears to yield energy for growth. Purification and partial characterization of the arsenite oxidase revealed that it (1). contains two heterologous subunits, AroA (86 kDa) and AroB (16 kDa), (2). has a native molecular mass of 306 kDa suggesting an alpha(3)beta(3) configuration, and (3). contains molybdenum and iron as cofactors. Although the Hydrogenophaga sp. str. NT-14 arsenite oxidase shares similarities to the arsenite oxidases purified from NT-26 and Alcaligenes faecalis, it differs with respect to activity and overall conformation. A c-551-type cytochrome was purified from Hydrogenophaga sp. str. NT-14 and appears to be the physiological electron acceptor for the arsenite oxidase. The cytochrome can also accept electrons from the purified NT-26 arsenite oxidase. A hypothetical electron transport chain for heterotrophic arsenite oxidation is proposed. |
Databáze: | OpenAIRE |
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