Biochemistry Seminar: Rachel Narhood Austin, "Exploring the structure and function of alkane monooxygenase (AlkB): A key metalloenzyme in the carbon cycle"

Dates
Wed, Dec 06, 2023 - 12:00 PM — Wed, Dec 06, 2023 - 01:00 PM
Admission Fee
Free. Coffee & tea will be available in the ASRC Cafe at 11:30 AM.
Event Address
This seminar is being given by Zoom ONLY. Zoom link: https://gc-cuny.zoom.us/j/96677631144. Pass code asrc-ccny
Phone Number
212-650-8803
Event Location
The Zoom broadcast may also be viewed in the ASRC Main auditorium at 85 Saint Nicholas Terrace.
Event Details

Rachel Narhood Austin, Professor, Department of Chemistry, Barnard College, Columbia University, will give a talk titled, "Exploring the structure and function of alkane monooxygenase (AlkB): a key metalloenzyme in the carbon cycle."

 

 

Zoom link: https://gc-cuny.zoom.us/j/96677631144. Meeting ID:  966 776 31144. Passcode: asrc-ccny

Rachel Narhood Austin, Professor, Department of Chemistry, Barnard College, will be giving a talk on "Exploring the structure and function of alkane monooxygenase (AlkB): A key metalloenzyme in the carbon cycle."

ABSTRACT

Alkane hydroxylase (AlkB) is a membrane-spanning non-heme diiron enzyme with a histidine-rich coordination site, first identified 50 years ago, responsible for catalyzing the hydroxylation of the majority of medium-to-long straight chain alkanes in the environment. AlkB catalyzes the hydroxylation of terminal alkanes, the epoxidation of alkenes, and, in selected cases, the desaturation of alkanes.  Despite its importance in the global carbon cycle, relatively little is known about this large and widely-distributed class of hydroxylases.  We have studied the reaction mechanism and substrate specificity of AlkB from Pseudomonas putida GPo1, the marine organism Alcanivorax borkumensis AP1, Dietzea cinnamea, and Fontimonas thermophila. We have recently solved the cryo-EM structure of AlkB from Fontimonas thermophila.  Integrating information from targeted mutations, reactivity studies, and the three-dimensional structure has shed light on structure-function relationships in this important class of integral membrane monooxygneases, while raising additional questions to be solved. 

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