The influence of structural variations in the F- and FG-helix of the β-subunit modified oxyHb-NES on the heme structure detected by resonance Raman spectroscopy-Reference-Cited by-同舟云学术

The influence of structural variations in the F- and FG-helix of the β-subunit modified oxyHb-NES on the heme structure detected by resonance Raman spectroscopy

Published:1989-06 Issue:2 Volume:17 Page:87-100
ISSN:0175-7571
Container-title:European Biophysics Journal
language:en
Short-container-title:Eur Biophys J

Author:

Schweitzer-Stenner R.,Wedekind D.,Dreybrodt W.

Publisher

Springer Science and Business Media LLC

Subject

General Medicine,Biophysics

Link

http://link.springer.com/content/pdf/10.1007/BF00257106.pdf

Reference34 articles.

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3. Brunner H, Mayer A, Sussner H (1972) Resonance Raman scattering on the Haem Group of Oxy- and Deoxyhaemoglobin. J Mol Biol 70:153–156

4. Brunzel U, Dreybrodt W, Schweitzer-Stenner R (1986) pH-dependent absorption in the B-and Q bands of oxyhemoglobin and chemically modified oxyhemoglobin (BME) at low Cl−-concentration. Biophys J 49:1069–1076

5. De Young A, Pennely R, Tan-Wilson A, Noble RW (1976) Kinetic studies on the binding affinity of human hemoglobin for the 4th carbon monoxide molecule L4. J Biol Chem 251:6692–6698

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