Abstract
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.
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