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Literature summary for 1.14.14.18 extracted from

  • Peng, D.; Ogura, H.; Zhu, W.; Ma, L.H.; Evans, J.P.; Ortiz de Montellano, P.R.; La Mar, G.N.
    Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase (2009), Biochemistry, 48, 11231-11242.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
265-residue constructs of wild-type and mutant D140A Homo sapiens

Protein Variants

Protein Variants Comment Organism
D140A exhibits resolved and relaxed 2,4-dimethyldeuterohemin resonances at low pH and at high pH Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

pH Stability

pH Stability pH Stability Maximum Comment Organism
10.3
-
sequential Ni-Ni+1 connections for Ile57-Ala60, His84-Lys86, Leu93-Trp96, and Leu164-Phe167 can be observed even at pH 10.3, with chemical shift similar to those for heme oxygenase-2,4-dimethyldeuterohemin-H2O Homo sapiens

Cofactor

Cofactor Comment Organism Structure
heme high-spin heme oxygenase-2,4-dimethyldeuterohemin-H2O complex dominates at low pH, low-spin heme oxygenase-2,4-dimethyldeuterohemin-OH complex dominates at alkaline pH Homo sapiens