5ILP

H64Q sperm whale myoglobin with a Fe-tolyl moiety

Summary for 5ILP

• Entry DOI: 10.2210/pdb5ilp/pdb
• Related: 5IKS 5ILE 5ILM 5ILR
• Descriptor: Myoglobin, [3,3'-(7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-diyl-kappa~4~N~21~,N~22~,N~23~,N~24~)di(propanoato)(2-)](3-methylphenyl)iron, SULFATE ION, ... (5 entities in total)
• Functional Keywords: bioorganometallic, heme, myoglobin, sigma-aryl, hydrazine, arylhydrazine, phenylhydrazine, iron-carbon, 3-methylphenylhydrazine, meta-tolylhydrazine, 4-chlorophenylhydrazine, para-chlorophenylhydrazine, oxygen transport
• Biological source: Physeter catodon (Sperm whale)
• Total number of polymer chains: 1
• Total formula weight: 18443.05

Authors

Wang, B.,Thomas, L.M.,Richter-Addo, G.B. (deposition date: 2016-03-04, release date: 2016-09-21, Last modification date: 2023-09-27)

Primary citation

Wang, B.,Thomas, L.M.,Richter-Addo, G.B.
Organometallic myoglobins: Formation of Fe-carbon bonds and distal pocket effects on aryl ligand conformations.
J. Inorg. Biochem., 164:1-4, 2016

PubMed Abstract: 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 1.7-1.9Å resolution. The structures reveal conformational preferences for the substituted aryls resulting from attachment of the aryl ligands to Fe at the site of net -NHNH release from the precursor hydrazines, and show distal pocket changes that readily accommodate these bulky ligands.

PubMed: 27687333
DOI: 10.1016/j.jinorgbio.2016.06.028

Experimental method

X-RAY DIFFRACTION (1.88 Å)