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. 1978 Dec;75(12):5755–5759. doi: 10.1073/pnas.75.12.5755

Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins.

G N La Mar, D L Budd, D B Viscio, K M Smith, K C Langry
PMCID: PMC393052  PMID: 282600

Abstract

A proton NMR method is described for determining the orientation of a porphyrin within the heme pocket of a hemoprotein. The pattern of the hyperfine-shifted heme methyl resonances in low-spin ferric model compounds is demonstrated to characteristically reflect the position of a localized low-symmetry perturbation on the pi system. The specific assignments via deuteration of the two interconvertible sets of methyl resonances observed for deuteroporphyrin-reconstituted sperm whale metmyoglobin cyanide lead to the conclusion that the low-symmetry perturbations on the heme due to the apo-protein contacts differ for the two protein components by a 180 degrees rotation about the alpha-gamma meso axis. Hence the heme in the reconstituted myoglobin is "disordered" in solution, and the altered functional properties of the reconstituted protein cannot be simply attributed to the local effect of the heme substituent. This NMR technique has applicability for determining the relative heme orientation in related hemoproteins, and may clarify the origin of doubling of heme resonances observed in several native hemoproteins.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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