Probing the Excited State of Methylcobalamin Using Polarized Time-Resolved X‑ray Absorption Spectroscopy

We use picosecond time-resolved polarized X-ray absorption near-edge structure (XANES) measurements to probe the structure of the long-lived photoexcited state of methylcobalamin (MeCbl) and the cob­(II)­alamin photoproduct formed following photoexcitation of adenosylcobalamin (AdoCbl, coenzyme B12)...

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Veröffentlicht in:The journal of physical chemistry. B 2019-07, Vol.123 (28), p.6042-6048
Hauptverfasser: Michocki, Lindsay B, Miller, Nicholas A, Alonso-Mori, Roberto, Britz, Alexander, Deb, Aniruddha, Glownia, James M, Kaneshiro, April K, Konar, Arkaprabha, Koralek, Jake, Meadows, Joseph H, Sofferman, Danielle L, Song, Sanghoon, Toda, Megan J, van Driel, Tim B, Kozlowski, Pawel M, Kubarych, Kevin J, Penner-Hahn, James E, Sension, Roseanne J
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Sprache:eng
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Zusammenfassung:We use picosecond time-resolved polarized X-ray absorption near-edge structure (XANES) measurements to probe the structure of the long-lived photoexcited state of methylcobalamin (MeCbl) and the cob­(II)­alamin photoproduct formed following photoexcitation of adenosylcobalamin (AdoCbl, coenzyme B12). For MeCbl, we used 520 nm excitation and a time delay of 100 ps to avoid the formation of cob­(II)­alamin. We find only small spectral changes in the equatorial and axial directions, which we interpret as arising from small (
ISSN:1520-6106
1520-5207
DOI:10.1021/acs.jpcb.9b05854