EC Number   |
|---|
  1.14.99.57 | cyanide-inhibited MhuD in complex with heme as well as detailed characterization of this species. There is no evidence for an ordered network of water molecules on the distal side of the heme substrate. The degree of heme ruffling in the crystal structure is greater than that observed for heme oxygenases and less than that observed for heme-degrading enzyme IsdI. The Fe 3dxz-, 3dyz-, and 3dxy-based molecular orbitals are very close in energy, and the room-temperature 1H NMR spectrum is consistent with population of both a 2Eg electronic state with a (dxy)2(dxz,dyz)3 electron configuration, and a 2B2g state with a (dxz,dyz)4(dxy)1 electron configuration. MhuD-heme-CN has a 2B2g electronic ground state with a low-lying 2Eg excited state |
| 1.14.99.57 | MhuD-diheme complex, to 1.75 A resolution, reveals two stacked hemes forming extensive contacts with residues in the active site. The solvent-exposed heme is axially liganded by His75 and is stacked planar upon the solvent-protected heme. The solvent-protected heme is coordinated by a chloride ion which is, in turn, stabilized by residue Asn7 |
| 1.14.99.57 | the catalytically active 1:1 heme-MhuD complex has an active site structure similar to those of heme degrading enzymes IsdG and IsdI, including the nonplanarity (ruffling) of the heme group bound to the enzyme |
