Associated Papers
Ferrochelatase π-helix: Implications from examining the role of the conserved π-helix glutamates in porphyrin metalation and product release.
Gillam ME et al.
Archives of Biochemistry and Biophysics, 2018
Investigation by MD simulation of the key residues related to substrate-binding and heme-release in human ferrochelatase.
Wang Y et al.
Journal of Molecular Modeling, 2013
Identification and characterization of solvent-filled channels in human ferrochelatase.
Medlock AE et al.
Biochemistry, 2012
A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase.
Medlock AE et al.
Journal of Molecular Biology, 2007
Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis.
Dailey HA et al.
Biochemistry, 2007
Substrate interactions with human ferrochelatase.
Medlock A et al.
Proceedings of the National Academy of Sciences of the United States of America, 2007
Production and characterization of erythropoietic protoporphyric heterodimeric ferrochelatases.
Najahi-Missaoui W et al.
Blood, 2005
Human ferrochelatase: characterization of substrate-iron binding and proton-abstracting residues.
Sellers VM et al.
Biochemistry, 2001
The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis.
Wu CK et al.
Nature Structural Biology, 2001
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