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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2009-1-27
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pubmed:databankReference |
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pubmed:abstractText |
Flavin C4a-OO(H) and C4a-OH adducts are critical intermediates proposed in many flavoenzyme reaction mechanisms, but they are rarely detected even by rapid transient kinetics methods. We observe a trapped flavin C4a-OH or C4a-OO(H) adduct by single-crystal spectroscopic methods and in the 1.86 A resolution X-ray crystal structure of choline oxidase. The microspectrophotometry results show that the adduct forms rapidly in situ at 100 K upon exposure to X-rays. Density functional theory calculations establish the electronic structures for the flavin C4a-OH and C4a-OO(H) adducts and estimate the stabilization energy of several active site hydrogen bonds deduced from the crystal structure. We propose that the enzyme-bound FAD is reduced in the X-ray beam. The aerobic crystals then form either a C4a-OH or C4a-OO(H) adduct, but an insufficient proton inventory prevents their decay at cryogenic temperatures.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-10576737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-10698731,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-10961912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-12586937,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-12817148,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-14678796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-14690428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-15288786,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-15362852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-15369826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-15649384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-15688436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-15713082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-16519539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-16600599,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-16627482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-16716069,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-16984920,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-17446401,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-17446402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-17683160,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-17959373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-18072756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-18652479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-3949735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-518869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-8077188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-816794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-8463299,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-8939867,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-915151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19133805-9628741
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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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 |
3
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pubmed:volume |
48
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
720-8
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pubmed:dateRevised |
2010-9-22
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pubmed:meshHeading |
pubmed-meshheading:19133805-Alcohol Oxidoreductases,
pubmed-meshheading:19133805-Arthrobacter,
pubmed-meshheading:19133805-Bacterial Proteins,
pubmed-meshheading:19133805-Binding Sites,
pubmed-meshheading:19133805-Computational Biology,
pubmed-meshheading:19133805-Crystallography, X-Ray,
pubmed-meshheading:19133805-Flavin-Adenine Dinucleotide,
pubmed-meshheading:19133805-Flavins,
pubmed-meshheading:19133805-Flavoproteins,
pubmed-meshheading:19133805-Oxygen,
pubmed-meshheading:19133805-Protein Structure, Secondary,
pubmed-meshheading:19133805-Spectrometry, X-Ray Emission
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pubmed:year |
2009
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pubmed:articleTitle |
Crystallographic, spectroscopic, and computational analysis of a flavin C4a-oxygen adduct in choline oxidase.
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pubmed:affiliation |
Biology Department, Brookhaven National Laboratory, Upton, New York 11973-5000, School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia 30332-0400, USA. amorv@bnl.gov
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pubmed:publicationType |
Journal Article,
Comparative Study,
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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