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Literature summary for 1.14.14.18 extracted from

  • Maines, M.D.; Kappas, A.
    Enzymatic oxidation of cobalt protoporphyrin IX: observations on the mechanism of heme oxygenase action (1977), Biochemistry, 16, 419-423.
    View publication on PubMed
Search for more literature for 1.14.14.18

Inhibitors

Inhibitors Comment Organism Structure
Porphyrins Ni, Mn, and Sn-protoporphyrin IX; overview Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.017
-
 Fe-heme
-
 Rattus norvegicus
0.125
-
 Co-heme
-
 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O mechanism Rattus norvegicus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Co-heme + NADPH + H+ + O2
-
 Rattus norvegicus biliverdin Ixalpha + Co2+ + CO + NAD+ + H2O
-
 r
Fe-heme + [reduced NADPH-hemoprotein reductase] + O2
-
 Rattus norvegicus biliverdin Ixalpha + Fe2+ + CO + NAD+ + H2O
-
 r
heme + electron donor + O2 overview, substrate specificity Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
 ?
heme + electron donor + O2 Ni, Mn, and Sn protoporphyrin IX is not oxidized Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
 ?
heme + electron donor + O2 oxidation of Co-heme Rattus norvegicus biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
 ?