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BY-NC-ND 3.0 license Open Access Published by De Gruyter June 2, 2014

ESR Studies on the Nitrosyl Complex of Hagfish (Myxine glutinosa L.) Hemoglobin

  • Maliyakal E. John , Ralte Lalthantluanga , Gisela Liljeqvist , Sven Paléusa and Gerhard Braunitzer

Abstract

The nitric oxide complex of hagfish hemoglobin exhibits electron spin resonance spectra centered around g = 2 with rhombic symmetry. The six coordinated spectrum is not influenced by protonation or presence of inositol hexaphosphate. Thus, the critical substitutions at E 7 (His → Gln) and E 11 (Yal → Ile) do not disrupt the proximal histidineiron bonds in the nitrosyl complex of this primitive hemoglobin, though the same type of substitution are known to cause destabilization of R quaternary structure in tetrameric mammalian nitrosylhemoglobins. This difference could be related to the difference in tension existing in the respective hemes of tetrameric and monomeric hemoglobins.

Received: 1981-3-27
Revised: 1981-3-1
Published Online: 2014-6-2
Published in Print: 1982-6-1

© 1946 – 2014: Verlag der Zeitschrift für Naturforschung

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

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