科技报告详细信息
Biochemistry of Ammonia Monoxygenase from Nitrosomonas
Alan Hooper
关键词: AMMONIA;    BACTERIA;    BIOCHEMISTRY;    CYTOCHROMES;    ELECTRON TRANSFER;    POTENTIOMETRY;    PROTEIN STRUCTURE;    PROTEINS;    PURIFICATION;    SIMULATION;    SPECTROSCOPY;   
DOI  :  10.2172/958735
RP-ID  :  DOE-ER/20191-1
PID  :  OSTI ID: 958735
Others  :  TRN: US201002%%984
学科分类:生物科学(综合)
美国|英语
来源: SciTech Connect
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【 摘 要 】

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.

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