Open AccessBiochemistry of Ammonia Monoxygenase from Nitrosomonas
Author(s) -
Alan B. Hooper
Publication year - 2009
Language(s) - English
Resource type - Reports
DOI - 10.2172/958735
Subject(s) - ammonia monooxygenase , ammonia , cytochrome , nitrosomonas europaea , chemistry , hemeprotein , monooxygenase , biochemistry , heme , beta (programming language) , ligand (biochemistry) , electron transfer , stereochemistry , cytochrome p450 , metabolism , organic chemistry , enzyme , nitrification , nitrogen , receptor , computer science , programming language , archaea , gene
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