Document Detail


The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.
MedLine Citation:
PMID:  16952937     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Utilization of heme by bacteria as a nutritional iron source involves the transport of exogenous heme, followed by cleavage of the heme macrocycle to release iron. Bradyrhizobium japonicum can use heme as an iron source, but no heme-degrading oxygenase has been described. Here, bioinformatics analyses of the B. japonicum genome identified two paralogous genes renamed hmuQ (bll7075) and hmuD (bll7423) that encode proteins with weak similarity to the heme-degrading monooxygenase IsdG from Staphylococcus aureus. The hmuQ gene is clustered with known heme transport genes in the genome. Recombinant HmuQ bound heme with a K(d) value of 0.8 microM and showed spectral properties consistent with a heme oxygenase. In the presence of a reductant, HmuQ catalyzed the degradation of heme and the formation of biliverdin. The hmuQ and hmuD genes complemented a Corynebacterium ulcerans heme oxygenase mutant in trans for utilization of heme as the sole iron source for growth. Furthermore, homologs of hmuQ and hmuD were identified in many bacterial genera, and the recombinant homolog from Brucella melitensis bound heme and catalyzed its degradation. The findings show that hmuQ and hmuD encode heme oxygenases and indicate that the IsdG family of heme-degrading monooxygenases is not restricted to gram-positive pathogenic bacteria.
Authors:
Sumant Puri; Mark R O'Brian
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural    
Journal Detail:
Title:  Journal of bacteriology     Volume:  188     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2006 Sep 
Date Detail:
Created Date:  2006-09-05     Completed Date:  2006-10-05     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  6476-82     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, 140 Farber Hall, State University of New York at Buffalo, Buffalo, NY 14214, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / chemistry,  genetics,  metabolism*
Biliverdine / metabolism
Bradyrhizobium / enzymology*,  genetics
Brucella melitensis / enzymology,  genetics
Computational Biology
Corynebacterium / genetics
Genes, Bacterial*
Genetic Complementation Test
Genome, Bacterial / genetics
Heme / metabolism*
Mixed Function Oxygenases / chemistry,  genetics,  metabolism*
Molecular Sequence Data
Multigene Family
Protein Binding
Recombinant Proteins / chemistry,  isolation & purification,  metabolism
Sequence Homology, Amino Acid
Spectrum Analysis
Staphylococcus aureus / genetics
Grant Support
ID/Acronym/Agency:
R01-GM067966/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Recombinant Proteins; 114-25-0/Biliverdine; 14875-96-8/Heme; EC 1.-/Mixed Function Oxygenases
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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