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| hmuOSummaryGene Symbol: hmuO Description: heme oxygenase Species: Top Publications
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Publications
Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobinM P Schmitt
Laboratory of Bacterial Toxins, Division of Bacterial Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Maryland 20892, USA
J Bacteriol 179:838-45. 1997..ulcerans mutants and three of the C. diphtheriae mutants. The nucleotide sequence of the gene (hmuO) required for complementation was determined and shown to encode a protein with a predicted mass of 24,123 Da...
Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriaeG C Chu
Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106 4970, USA
J Biol Chem 274:21319-25. 1999..However, the considerably slow catalytic rate and low level of verdoheme recovery in the hydrogen peroxide reaction suggest that the active-site structure of Hmu O is different from that of its mammalian counterpart...
The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriaeShoko Hirotsu
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira, Aoba, Sendai 980 8577, Japan
J Biol Chem 279:11937-47. 2004Crystal structures of the ferric and ferrous heme complexes of HmuO, a 24-kDa heme oxygenase of Corynebacterium diphtheriae, have been refined to 1.4 and 1.5 A resolution, respectively...
Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase functionMasaki Unno
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira, Aoba, Sendai 980 8577, Japan
J Biol Chem 279:21055-61. 2004b>HmuO, a heme oxygenase of Corynebacterium diphtheriae, catalyzes degradation of heme using the same mechanism as the mammalian enzyme...
Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanismToshitaka Matsui
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira, Aoba, Sendai 980 8577, Japan
J Biol Chem 280:2981-9. 2005..Roles of distal Asp (Asp-136) residue in HmuO, a heme oxygenase of Corynebacterium diphtheriae, have been investigated by site-directed mutagenesis, enzyme ..
Design of metal cofactors activated by a protein-protein electron transfer systemTakafumi Ueno
Research Center for Materials Science, Graduate School of Science, Nagoya University, Furo cho, Chikusa ku, Nagoya 464 8602, Japan
Proc Natl Acad Sci U S A 103:9416-21. 2006..Our Fe(Schiff-base).HO composite model system may provide insights with regard to design of ET biosystems for sensors, catalysts, and electronics devices...
NMR assignments of cd-HO, a 24 kDa heme oxygenase from Corynebacterium diphtheriaKELLIE HOM
Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, 20 Penn Street, Baltimore, MD 21201, USA
Biomol NMR Assign 1:55-6. 2007....
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexesZhenming Du
Department of Chemistry, University of California, Davis, CA 95616, USA
J Inorg Biochem 104:1063-70. 2010..structure upon substrate loss for the heme oxygenase from the pathogenic bacterium Corynebacterium diphtheriae, HmuO. The chemical shifts for the conserved portion of the structure are assessed as references for the dipolar shifts ..
