Resonance raman characterization of a novel, oxygen-binding heme protein from Chromatum vinosum
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference31 articles.
1. Isolation and characterization of two soluble heme c-containing proteins from Chromatium vinosum
2. Iron-ligand stretching band in the resonance Raman spectra of ferrous iron porphyrin derivatives. Importance as a probe band for quaternary structure of hemoglobin
3. Assignment of the Fe-Nϵ (His F8) stretching band in the resonance Raman spectra of deoxy myoglobin
4. Resonance Raman spectra of the heme in leghemoglobin. Evidence for the absence of ruffling and the influence of the vinyl groups.
5. Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteins
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. Transmutation of a heme protein.;Proceedings of the National Academy of Sciences;1993-07-15
2. Iron (1984);Coordination Chemistry Reviews;1992-03
3. Resonance Raman characterization of Chromatium vinosum cytochrome c'. Effect of pH and comparison of equilibrium and photolyzed carbon monoxide species;Biochemistry;1990-05-01
4. Spectroscopic and ligand-binding properties of an oxygen-binding heme protein from Chromatium vinosum;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1988-01
5. Spectroscopic and kinetic properties of an oxygen-binding heme protein from Chromatium vinosum.;Journal of Biological Chemistry;1987-01
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