Structural highlights
Function
[MYG_PHYCD] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Publication Abstract from PubMed
Bioorganometallic Fe-C bonds are biologically relevant species that may result from the metabolism of natural or synthetic hydrazines. The molecular structures of four new sperm whale mutant myoglobin derivatives with Fe-aryl moieties, namely H64A-tolyl-m, H64A-chlorophenyl-p, H64Q-tolyl-m, and H64Q-chlorophenyl-p, have been determined at 1.7-1.9A resolution. The structures reveal conformational preferences for the substituted aryls resulting from attachment of the aryl ligands to Fe at the site of net -NHNH2 release from the precursor hydrazines, and show distal pocket changes that readily accommodate these bulky ligands.
Organometallic myoglobins: Formation of Fe-carbon bonds and distal pocket effects on aryl ligand conformations.,Wang B, Thomas LM, Richter-Addo GB J Inorg Biochem. 2016 Jun 24. pii: S0162-0134(16)30192-1. doi:, 10.1016/j.jinorgbio.2016.06.028. PMID:27687333[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang B, Thomas LM, Richter-Addo GB. Organometallic myoglobins: Formation of Fe-carbon bonds and distal pocket effects on aryl ligand conformations. J Inorg Biochem. 2016 Jun 24. pii: S0162-0134(16)30192-1. doi:, 10.1016/j.jinorgbio.2016.06.028. PMID:27687333 doi:http://dx.doi.org/10.1016/j.jinorgbio.2016.06.028
