Biochemistry of Ammonia Monoxygenase from Nitrosomonas [electronic resource].
- Washington, D.C. : United States. Dept. of Energy. Office of Energy Research, 2009. and Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy.
- Physical Description:
- 40 KB : digital, PDF file
- Additional Creators:
- United States. Department of Energy. Office of Energy Research and United States. Department of Energy. Office of Scientific and Technical Information
- Restrictions on Access:
- Free-to-read Unrestricted online access
- Major results. 1. CytochromecM552, a protein in the electron transfer chain to ammonia monooxygenase. Purification, modeling of protein structure based on primary structure, characterization of 4 hemes by magnetic spectroscopy, potentiometry, ligand binding and turnover. Kim, H. J., ,Zatsman, et al. 2008). 2. Characterization of proteins which thought to be involved in the AMO reaction or to protect AMO from toxic nitrogenous intermediates such as NO. Nitrosocyanin is a protein present only in bacteria which catalyze the ammonia monoxygenase reaction (1). Cytochrome c P460 beta and cytochrome c’ beta.
- Published through SciTech Connect., 07/15/2009., "doe-er/20191-1", Alan Hooper., and Alan B. Hooper
- Type of Report and Period Covered Note:
- Final; 08/01/1995 - 07/31/2008
- Funding Information:
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