Structural determinants for the formation of sulfhemeprotein complexes.
Several hemoglobins were explored by UV-Vis and resonance Raman spectroscopy to define sulfheme complex formation. Evaluation of these proteins upon the reaction with H(2)O(2) or O(2) in the presence of H(2)S suggest: (a) the formation of the sulfheme derivate requires a HisE7 residue in the heme distal site with an adequate orientation to form an active ternary complex; (b) that the ternary complex intermediate involves the HisE7, the peroxo or ferryl species, and the H(2)S molecule. This moiety precedes and triggers the sulfheme formation.
Román-Morales
Elddie
E
Department of Chemistry, University of Puerto Rico, Mayagüez Campus, P.O. Box 9019, Mayagüez, Puerto Rico 00681-9019, Puerto Rico.
Pietri
Ruth
R
Ramos-Santana
Brenda
B
Vinogradov
Serge N
SN
Lewis-Ballester
Ariel
A
López-Garriga
Juan
J
D000818:Animals; D006418:Heme / Q000737:chemistry; D006639:Histidine / Q000737:chemistry*; D006801:Humans; D006862:Hydrogen Sulfide / Q000737:chemistry*; D010100:Oxygen / Q000737:chemistry*; D013059:Spectrum Analysis, Raman; D013435:Sulfhemoglobin / Q000737:chemistry*; D014867:Water / Q000737:chemistry*; D014907:Whales
D014867:Water; D006418:Heme; D006639:Histidine; D013435:Sulfhemoglobin; D010100:Oxygen; D006862:Hydrogen Sulfide