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. Author manuscript; available in PMC: 2015 Apr 1.
Published in final edited form as: J Inorg Biochem. 2014 Jan 25;133:78–86. doi: 10.1016/j.jinorgbio.2014.01.013

Figure 1.

Figure 1

Distal active site of: (a) L. pectinata (PDB:1MOH), (b) R. pachyptila (PDB: 1YHU), (c) O. mashikoi (PBD:2ZS0), and (d)L. terrestris (PDB:1X9F). In L. pectinata, H2S (shown as the sphere) binds to the ferric heme iron. R. pachyptila and O. mashikoi bind H2S in the free Cys residue and O2 in the heme iron center shown as spheres. In L. terrestris, the Cys residue is replaced by Leu, and in the presence of O2, H2S diffuses through the protein without encountering alternative binding sites and once at the heme site, it can interact directly with heme forming the sulfheme derivative.