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Optical inter-site spin transfer probed by energy and spin-resolved transient absorption spectroscopy.

ABSTRACT: Optically driven spin transport is the fastest and most efficient process to manipulate macroscopic magnetization as it does not rely on secondary mechanisms to dissipate angular momentum. In the present work, we show that such an optical inter-site spin transfer (OISTR) from Pt to Co emerges as a dominant mechanism governing the ultrafast magnetization dynamics of a CoPt alloy. To demonstrate this, we perform a joint theoretical and experimental investigation to determine the transient changes of the helicity dependent absorption in the extreme ultraviolet spectral range. We show that the helicity dependent absorption is directly related to changes of the transient spin-split density of states, allowing us to link the origin of OISTR to the available minority states above the Fermi level. This makes OISTR a general phenomenon in optical manipulation of multi-component magnetic systems.

SUBMITTER: Willems F

PROVIDER: S-EPMC7018696 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature

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Optical inter-site spin transfer probed by energy and spin-resolved transient absorption spectroscopy.

Willems Felix F von Korff Schmising Clemens C Strüber Christian C Schick Daniel D Engel Dieter W DW Dewhurst J K JK Elliott Peter P Sharma Sangeeta S Eisebitt Stefan S

Nature communications 20200213 1

Optically driven spin transport is the fastest and most efficient process to manipulate macroscopic magnetization as it does not rely on secondary mechanisms to dissipate angular momentum. In the present work, we show that such an optical inter-site spin transfer (OISTR) from Pt to Co emerges as a dominant mechanism governing the ultrafast magnetization dynamics of a CoPt alloy. To demonstrate this, we perform a joint theoretical and experimental investigation to determine the transient changes ...[more]

PMID: 32054855

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Project description:The quantum yield and kinetics of decay of cob(II)alamin formed by pulsed-laser photolysis of adenosylcobalamin (AdoCbl; coenzyme B(12)) in AdoCbl-dependent ethanolamine ammonia-lyase (EAL) from Salmonella typhimurium have been studied on the 10(-7)-10(-1) s time scale at 295 K by using transient ultraviolet-visible absorption spectroscopy. The aim is to probe the mechanism of formation and stabilization of the cob(II)alamin-5'-deoxyadenosyl radical pair, which is a key intermediate in EAL catalysis, and the influence of substrate binding on this process. Substrate binding is required for cobalt-carbon bond cleavage in the native system. Photolysis of AdoCbl in EAL leads to a quantum yield at 10(-7) s for cob(II)alamin of 0.08 +/- 0.01, which is 3-fold smaller than for AdoCbl in aqueous solution (0.23 +/- 0.01). The protein binding site therefore suppresses photoproduct radical pair formation. Three photoproduct states, P(f), P(s), and P(c), are identified in holo-EAL by the different cob(II)alamin decay kinetics (subscripts denote fast, slow, and constant, respectively). These states have the following first-order decay rate constants and quantum yields: 2.2 x 10(3) s(-1) and 0.02 for P(f), 4.2 x 10(2) s(-1) and 0.01 for P(s), and constant amplitude, with no recombination, and 0.05 for P(c), respectively. Binding of the substrate analogue (S)-1-amino-2-propanol to EAL eliminates the P(f) state and lowers the quantum yield of P(c) (0.03) relative to that of P(s) (0.01) but does not significantly change the quantum yield or decay rate constant of P(s), relative to those of holo-EAL. The substrate analogue thus influences the quantum yield at 10(-7) s by changing the cage escape rate from the geminate cob(II)alamin-5'-deoxyadenosyl radical pair state. However, the predicted substrate analogue binding-induced increase in the quantum yield is not observed. It is proposed that the substrate analogue does not induce the radical pair stabilizing changes in the protein that are characteristic of true substrates.

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Optical inter-site spin transfer probed by energy and spin-resolved transient absorption spectroscopy.

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Optical inter-site spin transfer probed by energy and spin-resolved transient absorption spectroscopy.

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