Event Website
http://www.bates.edu/mt-david-summit.xml
Start Date
1-4-2011 1:45 PM
End Date
1-4-2011 3:00 PM
Description
The non-heme diiron monooxygenase ω-Alkane Hydroxylase (AlkB) is a membrane spanning metalloenzyme that is the first step in the catabolism of medium length alkanes in a variety of hydrocarbon dependent organisms. The marine organism Alcanivorak borkumensis AP1 is the source of AlkB used in this study. The protein was purified using Fast Protein Liquid Chromatography (FPLC) and then magnetic circular dichroism (MCD) was used to gain spectroscopic data on the diiron active site, which contains predominantly histidines as the metal ligands. These data provide continued insight in respect to the theory that a single atom magnetically links the two iron ions.
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A MCD Study of the Diiron Active Site of ω-Alkane Hydroxylase (AlkB)
The non-heme diiron monooxygenase ω-Alkane Hydroxylase (AlkB) is a membrane spanning metalloenzyme that is the first step in the catabolism of medium length alkanes in a variety of hydrocarbon dependent organisms. The marine organism Alcanivorak borkumensis AP1 is the source of AlkB used in this study. The protein was purified using Fast Protein Liquid Chromatography (FPLC) and then magnetic circular dichroism (MCD) was used to gain spectroscopic data on the diiron active site, which contains predominantly histidines as the metal ligands. These data provide continued insight in respect to the theory that a single atom magnetically links the two iron ions.
http://scarab.bates.edu/mt_david_summit/MDS2011/02Poster/17