Identification of the Hydrophobic Amino Acid Residues Required for Heme Assembly in the Rhizobial Oxygen Sensor Protein FixL-Reference-Cited by-同舟云学术

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Identification of the Hydrophobic Amino Acid Residues Required for Heme Assembly in the Rhizobial Oxygen Sensor Protein FixL

Published:1998-06 Issue:2 Volume:247 Page:427-431
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Nakamura Hiro,Saito Ken,Ito Eiichi,Tamura Koji,Tsuchiya Terumasa,Nishigaki Koichi,Shiro Yoshitsugu,Iizuka Tetsutaro

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference22 articles.

1. Protein phosphorylation and regulation of adaptive responses in bacteria

2. Genetic regulation of nitrogen fixation in rhizobia

3. A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti

4. Heme-Based Sensors, Exemplified by the Kinase FixL, Are a New Class of Heme Protein with Distinctive Ligand Binding and Autoxidation

5. Cascade regulation of nif gene expression in Rhizobium meliloti

Cited by 23 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Ultraviolet Resonance Raman Observations of the Structural Dynamics of Rhizobial Oxygen Sensor FixL on Ligand Recognition;The Journal of Physical Chemistry B;2013-08-26

2. Amyloid beta modulated the selectivity of heme-catalyzed protein tyrosine nitration: an alternative mechanism for selective protein nitration;JBIC Journal of Biological Inorganic Chemistry;2012-07-21

3. Amyloid beta–heme peroxidase promoted protein nitrotyrosination: relevance to widespread protein nitration in Alzheimer’s disease;JBIC Journal of Biological Inorganic Chemistry;2011-09-14

4. Phosphate-Affinity Gel Electrophoresis Using a Phos-Tag Molecule for Phosphoproteome Study;Current Proteomics;2009-07-01

5. Role of Phe113 at the distal side of the heme domain of an oxygen-sensor (Ec DOS) in the characterization of the heme environment;Journal of Inorganic Biochemistry;2009-07

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