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Abstract
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Article Information:
Spectroscopic Investigation of Pyruvate Formate Lyase-activating Enzyme: A Look into EPR, ENDOR and Mössabuer Spectroscopy
Danilo O. Ortillo and Joan B. Broderick
Corresponding Author: Danilo O. Ortillo
Submitted: April 08, 2014
Accepted: April 28, 2014
Published: September 05, 2014 |
Abstract:
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Electron Paramagnetic Resonance (EPR) and Electron Nuclear Double Resonance (ENDOR) spectroscopies are extremely powerful and versatile methods for the characterization of paramagnetic systems in biology, chemistry and physics. For iron centers in the radical SAM enzymes however, Mössbauer spectroscopy has proven to be both powerful and useful as a complementary spectroscopic technique in determining not just the oxidation states but also the type of iron species present in the catalytic center. The cluster content of the radical SAM protein, Pyruvate Formate-Lyase-Activating Enzyme (PFL-AE), was characterized using EPR and Mössbauer techniques while additional ENDOR analysis helped determine the novel interaction of the co-substrate, S-Adenosylmethionine (SAM or AdoMet) with the Fe-S cluster of PFL-AE. The anchoring role of the Fe-S cluster to the co-substrate derived from the spectroscopic data supports the mechanism where a SAM-based radical species is involved during catalysis.
Key words: AdoMet, pyruvate formate-lyase-activating enzyme, radical SAM, spectroscopic methods, , ,
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Cite this Reference:
Danilo O. Ortillo and Joan B. Broderick, . Spectroscopic Investigation of Pyruvate Formate Lyase-activating Enzyme: A Look into EPR, ENDOR and Mössabuer Spectroscopy. Research Journal of Applied Sciences, Engineering and Technology, (9): 1075-1097.
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ISSN (Online): 2040-7467
ISSN (Print): 2040-7459 |
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