1997
DOI: 10.1021/bi962321m
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Histidine-132 Does Not Stabilize a Distal Water Ligand and Is Not an Important Residue for the Enzyme Activity in Heme Oxygenase-1

Abstract: Heme oxygenase is a key enzyme in the oxygen-dependent heme catabolism pathway. In order to clarify the role of highly conserved His132 in heme oxygenase isoform-1, we have prepared 30 kDa truncated rat heme oxygenase mutants in which His132 has been replaced by Ala, Gly, and Ser. The expressed recombinant mutant proteins were isolated in inclusion bodies and were recovered from the lysis pellet by dissolution in urea followed by dialysis. The solubilized fraction obtained, however, was composed of a mixture o… Show more

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Cited by 46 publications
(22 citation statements)
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References 23 publications
(51 reference statements)
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“…This phenomenon was observed with other, eukaryotic heme oxygenases and C. diphtheriae HmuO when they were overexpressed in E. coli (4,55). (1997) did not confirm the role of His-132 in heme degradation (23). The corresponding part of neisserial proteins is not well conserved and contains a tryptophan residue instead of a histidine at position 132.…”
Section: Discussionmentioning
confidence: 95%
“…This phenomenon was observed with other, eukaryotic heme oxygenases and C. diphtheriae HmuO when they were overexpressed in E. coli (4,55). (1997) did not confirm the role of His-132 in heme degradation (23). The corresponding part of neisserial proteins is not well conserved and contains a tryptophan residue instead of a histidine at position 132.…”
Section: Discussionmentioning
confidence: 95%
“…Bacterial and mammalian HOs use the CPR-NADPH system, ferredoxin, flavodoxin, or ascorbic acid as reducing partners in vitro (11,34,(38)(39)(40)(41). To effectively monitor and quantify the HO activity of ChuS, 50 M ascorbic acid was used.…”
Section: Resultsmentioning
confidence: 99%
“…Although the overall similarity is only 20-30% between AtHO1 and 2 and the related HOs, a number of conserved amino acid clusters can be seen throughout their coding regions. One cluster contains a positionally conserved His (His-198 in AtHO1) shown to be important for structural stability in human HOs (43). A second cluster near the N terminus of human HOs (residues 76-96 in AtHO1) is required for the oxidative cleavage and employs a His to bind the heme substrate (44).…”
Section: Resultsmentioning
confidence: 99%