Structures of thiolate- and carboxylate-ligated ferric H93G myoglobin: models for cytochrome P450 and for oxyanion-bound heme proteins

Biochemistry
Jie QinLukasz Lebioda

Abstract

Crystal structures of the ferric H93G myoglobin (Mb) cavity mutant containing either an anionic proximal thiolate sulfur donor or a carboxylate oxygen donor ligand are reported at 1.7 and 1.4 A resolution, respectively. The crystal structure and magnetic circular dichroism spectra of the H93G Mb beta-mercaptoethanol (BME) thiolate adduct reveal a high-spin, five-coordinate complex. Furthermore, the bound BME appears to have an intramolecular hydrogen bond involving the alcohol proton and the ligated thiolate sulfur, mimicking one of the three proximal N-H...S hydrogen bonds in cytochrome P450. The Fe is displaced from the porphyrin plane by 0.5 A and forms a 2.41 A Fe-S bond. The Fe(3+)-S-C angle is 111 degrees , indicative of a covalent Fe-S bond with sp(3)-hybridized sulfur. Therefore, the H93G Mb.BME complex provides an excellent protein-derived structural model for high-spin ferric P450. In particular, the Fe-S bond in high-spin ferric P450-CAM has essentially the same geometry despite the constraints imposed by covalent linkage of the cysteine to the protein backbone. This suggests that evolution led to the geometric optimization of the proximal Fe-S(cysteinate) bond in P450. The crystal structure and spectral properties o...Continue Reading

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Citations

Apr 2, 2008·Inorganic Chemistry·Yongying Jiang, Paul R Ortiz de Montellano
Jun 11, 2009·Proceedings of the National Academy of Sciences of the United States of America·Elaine R Frawley, Robert G Kranz
Nov 30, 2012·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Xiao HuangLukasz Lebioda
Jul 23, 2009·Archives of Biochemistry and Biophysics·Enrica DroghettiGiulietta Smulevich
Nov 6, 2014·Acta Crystallographica. Section D, Biological Crystallography·Chunxue WangLukasz Lebioda

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