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Chemistry Seminar Program
Inorganic Chemistry Seminar Tuesday, February 27th Professor Michael Green “Understanding C-H Bond Activation in Heme Proteins”  4:15pm - 5:15pm Braun Lecture Hall S.G.Mudd Chemistry Building Stanford University This seminar is free and open to the public. All Stanford University Chemistry students are encouraged to attend this special event. About the seminar: Cytochrome P450’s are hydroxylating thiolate-ligated heme proteins that play critical roles in the production of hormones and the metabolism of xenobiotics. The human enzyme CYP2B6, for example, has been implicated in the metabolism of bupropion (depression, ADHD), ifosfamide (cervical cancer), tamoxifen (breast cancer), selegiline (Parkinson’s), rifampicin (tuberculosis), and nicotine. Interest in P450’s stems not only from their biological importance but also from a desire to harness their synthetic potential. P450’s can insert an oxygen atom derived from either peroxide or molecular oxygen into unactivated C-H bonds. Recently, we have shown that the iron(IV)oxo (ferryl) species found in P450’s and a related thiolate-ligated enzyme (chloroperoxidase) are basic, while those found in histidine-ligated enzymes (e.g. horseradish peroxidase, cytochrome c peroxidase, and myoglobin) are not. The Fe(IV)OH species in CPO and P450 are unusual: No synthetic or mineral iron-hydroxide above the ferric state has been structurally characterized, and no signal directly associated with the proton of an Fe(IV)OH center has ever been reported. We have recently located spectroscopic signals directly attributable to the hydroxide proton of CPO-II. Our findings provide the first direct evidence for the existence of an iron(IV)hydroxide in any chemical system. These results and their implications for C-H bond activation will be discussed. About Green:
Questions: Please contact Patricia Dwyer at 650-723-4770.
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