Arsenite Oxidase, an Ancient Bioenergetic Enzyme
نویسندگان
چکیده
منابع مشابه
Genome Analysis of Structure–Function Relationships in Respiratory Complex I, an Ancient Bioenergetic Enzyme
Respiratory complex I (NADH:ubiquinone oxidoreductase) is a ubiquitous bioenergetic enzyme formed by over 40 subunits in eukaryotes and a minimum of 11 subunits in bacteria. Recently, crystal structures have greatly advanced our knowledge of complex I but have not clarified the details of its reaction with ubiquinone (Q). This reaction is essential for bioenergy production and takes place in a ...
متن کاملArsenite oxidase also functions as an antimonite oxidase.
Arsenic and antimony are toxic metalloids and are considered priority environmental pollutants by the U.S. Environmental Protection Agency. Significant advances have been made in understanding microbe-arsenic interactions and how they influence arsenic redox speciation in the environment. However, even the most basic features of how and why a microorganism detects and reacts to antimony remain ...
متن کاملErratum for Wang et al., Arsenite oxidase also functions as an antimonite oxidase.
Qian Wang, Thomas P. Warelow, Yoon-Suk Kang, Christine Romano, Thomas H. Osborne, Corinne R. Lehr, Brian Bothner, Timothy R. McDermott, Joanne M. Santini, Gejiao Wang State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan, People’s Republic of China; Institute of Structural & Molecular Biology, University College London, London, United Kingdom; Department of ...
متن کاملProtein film voltammetry of arsenite oxidase from the chemolithoautotrophic arsenite-oxidizing bacterium NT-26.
The chemolithoautotrophic bacterium NT-26 (isolated from a gold mine in the Northern Territory of Australia) is unusual in that it acquires energy by oxidizing arsenite to arsenate while most other arsenic-oxidizing organisms perform this reaction as part of a detoxification mechanism against the potentially harmful arsenite [present as As(OH)(3) at neutral pH]. The enzyme that performs this re...
متن کاملMolybdenum-containing arsenite oxidase of the chemolithoautotrophic arsenite oxidizer NT-26.
The chemolithoautotroph NT-26 oxidizes arsenite to arsenate by using a periplasmic arsenite oxidase. Purification and preliminary characterization of the enzyme revealed that it (i) contains two heterologous subunits, AroA (98 kDa) and AroB (14 kDa); (ii) has a native molecular mass of 219 kDa, suggesting an alpha2beta2 configuration; and (iii) contains two molybdenum and 9 or 10 iron atoms per...
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ژورنال
عنوان ژورنال: Molecular Biology and Evolution
سال: 2003
ISSN: 0737-4038,1537-1719
DOI: 10.1093/molbev/msg071