Hemeproteins
From NMR Wiki
(Hemoglobins, Myoglobins, Cytochromes, etc.)
Heme orientational disorder
Since the heme group is asymmetric, it can insert into the heme pocket in two ways. Such heme orientational disorder is sometimes observed in the heme proteins, e.g. neuroglobin[1], hemoglobin[2].
References
- Yamamoto, Y and La Mar, GN. Proton NMR study of dynamics and thermodynamics of heme rotational disorder in native and reconstituted hemoglobin A. Biochemistry 25(18):5288--5297, 1986. BibTeX
-
Alam, SL and Satterlee, JD. Unambiguous Heme Proton Hyperfine Resonance Assignments of a Monomeric Hemoglobin from Glycera dibranchiata Facilitated with a Completely Deuterated Protein. Journal of the American Chemical Society 117(1):49--53, 1995. BibTeX
-
Keller, R and Groudinsky, O and W{\"u}thrich, K. Contact-shifted resonances in the 1H NMR spectra of cytochrome b5. Resonance identification and spin density distribution in the heme group.. Biochimica et biophysica acta 427(2):497, 1976. BibTeX
-
Du, W and Syvitski, R and Dewilde, S and Moens, L and La Mar, GN. Solution 1H NMR characterization of equilibrium heme orientational disorder with functional consequences in mouse neuroglobin. J Am Chem Soc 125(27):8080--8081, 2003. BibTeX
