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. 1994 May 24;91(11):4723–4726. doi: 10.1073/pnas.91.11.4723

Three-dimensional structure of cyanomet-sulfmyoglobin C.

S V Evans 1, B P Sishta 1, A G Mauk 1, G D Brayer 1
PMCID: PMC43860  PMID: 8197124

Abstract

The atomic structure of horse heart cyanomet-sulfmyoglobin C has been established by x-ray crystallographic techniques to a resolution of 2.0 A with an R value of 0.129. The protoheme IX prosthetic group of this thermodynamically stable sulfmyoglobin derivative has been converted to a chlorin in which the pyrrole ring bearing the 4-vinyl group is saturated and possesses an exocyclic thiolene ring. This study provides the three-dimensional structure of a protein with an iron-chlorin prosthetic group. The overall conformation of the surrounding polypeptide chain of the modified protein is very similar to that of the native protein. However, the addition of the sulfur atom has caused a distortion of the prosthetic group from that in the native protein to result in the repositioning of the side chains of some residues in the heme pocket.

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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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