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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
2011-4-5
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pubmed:databankReference |
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pubmed:abstractText |
MauG is a diheme enzyme responsible for the post-translational formation of the catalytic tryptophan tryptophylquinone (TTQ) cofactor in methylamine dehydrogenase (MADH). MauG can utilize hydrogen peroxide, or molecular oxygen and reducing equivalents, to complete this reaction via a catalytic bis-Fe(IV) intermediate. Crystal structures of diferrous, Fe(II)-CO, and Fe(II)-NO forms of MauG in complex with its preMADH substrate have been determined and compared to one another as well as to the structure of the resting diferric MauG-preMADH complex. CO and NO each bind exclusively to the 5-coordinate high-spin heme with no change in ligation of the 6-coordinate low-spin heme. These structures reveal likely roles for amino acid residues in the distal pocket of the high-spin heme in oxygen binding and activation. Glu113 is implicated in the protonation of heme-bound diatomic oxygen intermediates in promoting cleavage of the O-O bond. Pro107 is shown to change conformation on the binding of each ligand and may play a steric role in oxygen activation by positioning the distal oxygen near Glu113. Gln103 is in a position to provide a hydrogen bond to the Fe(IV)?O moiety that may account for the unusual stability of this species in MauG.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Monoxide,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome-c Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Ferrous Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Hemeproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Indolequinones,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases Acting on CH-NH...,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/diheme cytochrome c,
http://linkedlifedata.com/resource/pubmed/chemical/methylamine dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/tryptophan tryptophylquinone
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1520-4995
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
12
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pubmed:volume |
50
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2931-8
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pubmed:meshHeading |
pubmed-meshheading:21355604-Amino Acid Sequence,
pubmed-meshheading:21355604-Bacterial Proteins,
pubmed-meshheading:21355604-Binding Sites,
pubmed-meshheading:21355604-Biocatalysis,
pubmed-meshheading:21355604-Carbon Monoxide,
pubmed-meshheading:21355604-Crystallography, X-Ray,
pubmed-meshheading:21355604-Cytochrome-c Peroxidase,
pubmed-meshheading:21355604-Ferrous Compounds,
pubmed-meshheading:21355604-Glutamic Acid,
pubmed-meshheading:21355604-Heme,
pubmed-meshheading:21355604-Hemeproteins,
pubmed-meshheading:21355604-Indolequinones,
pubmed-meshheading:21355604-Models, Chemical,
pubmed-meshheading:21355604-Models, Molecular,
pubmed-meshheading:21355604-Molecular Sequence Data,
pubmed-meshheading:21355604-Molecular Structure,
pubmed-meshheading:21355604-Nitric Oxide,
pubmed-meshheading:21355604-Oxidoreductases,
pubmed-meshheading:21355604-Oxidoreductases Acting on CH-NH Group Donors,
pubmed-meshheading:21355604-Oxygen,
pubmed-meshheading:21355604-Paracoccus denitrificans,
pubmed-meshheading:21355604-Protein Binding,
pubmed-meshheading:21355604-Protein Structure, Tertiary,
pubmed-meshheading:21355604-Sequence Homology, Amino Acid,
pubmed-meshheading:21355604-Spectrophotometry,
pubmed-meshheading:21355604-Substrate Specificity,
pubmed-meshheading:21355604-Tryptophan
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pubmed:year |
2011
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pubmed:articleTitle |
Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation.
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pubmed:affiliation |
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, 321 Church Street SE, Minneapolis, Minnesota 55455, United States.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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