E.p.r. studies of photolysis of nitrosyl haemoglobin at low temperatures: effects of quaternary structure
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,General Medicine,Biochemistry,Structural Biology
Reference29 articles.
1. Dynamics of ligand binding to myoglobin
2. Tunneling in Ligand Binding to Heme Proteins
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5. Rebinding and relaxation in the myoglobin pocket
Cited by 6 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. Ligand Binding Intermediates of Nitrosylated Human Hemoglobin Induced at Low Temperature by X-ray Irradiation;Inorganic Chemistry;2011-08-30
2. References;Dispersive Kinetics;2001
3. Low temperature photolysis of denatured nitrosyl hemoproteins;International Journal of Biological Macromolecules;1998-10
4. EPR Characterization of Nitric Oxide Binding to Hemoglobin;Nitric Oxide Research from Chemistry to Biology;1997
5. Low-temperature ESR studies on the photolysis of nitrosyl haemoglobin in aqueous solutions;Chemical Physics Letters;1995-01
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