NDLI: Ultrafast photochemistry of the bc<sub>1</sub> complex

Content Provider	Royal Society of Chemistry (RSC)
Author	Vos, Marten H. Reeder, Brandon J. Liebl, Ursula Daldal, Fevzi
Copyright Year	2017
Abstract	We present a full investigation of ultrafast light-induced events in the membraneous cytochrome bc1 complex by transient absorption spectroscopy. This energy-transducing complex harbors four redox-active components per monomer: heme c1, two 6-coordinate b-hemes and a [2Fe–2S] cluster. Using excitation of these components in different ratios under various excitation conditions, probing in the full visible range and under three well-defined redox conditions, we demonstrate that for all ferrous hemes of the complex photodissociation of axial ligands takes place and that they rebind in 5–7 ps, as in other 6-coordinate heme proteins, including cytoglobin, which is included as a reference in this study. By contrast, the signals are not consistent with photooxidation of the b hemes. This conclusion contrasts with a recent assessment based on a more limited data set. The binding kinetics of internal and external ligands are indicative of a rigid heme environment, consistent with the electron transfer function. We also report, for the first time, photoactivity of the very weakly absorbing iron–sulfur center. This yields the unexpected perspective of studying photochemistry, initiated by excitation of iron–sulfur clusters, in a range of protein complexes.
Starting Page	6807
Ending Page	6813
Page Count	7
File Format	HTM / HTML PDF
ISSN	14639076
Volume Number	19
Issue Number	9
Journal	Physical Chemistry Chemical Physics
DOI	10.1039/c7cp00193b
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Coenzyme Q \u2013 cytochrome c reductase Redox Cytoglobin Iron\u2013sulfur cluster Photodissociation Transfer function Protein Photochemistry
Content Type	Text
Resource Type	Article
Subject	Physics and Astronomy Physical and Theoretical Chemistry

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