Photoinduced transient absorbance spectra of P840/P840+ and the FMO protein in reaction centers of Chlorobium vibrioforme

Ilya R. Vassiliev, Bodil Kjær, Gregory L. Schorner, Henrik V. Scheller, John H. Golbeck

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Abstract

The kinetics of photoinduced absorbance change in the 400-ns to 100-ms time range were studied between 770 and 1025 nm in reaction center core (RCC) complexes isolated from the green sulfur bacterium Chlorobium vibrioforme. A global, multiple stretched-exponential analysis shows the presence of two distinct but strongly overlapping spectra. The spectrum of the 70-μs component consists of a broad bleaching with two minima at 810 and 825 nm and a broad positive band at wavelengths greater than 865 nm and is assigned to the decay of 3Bchl a of the Fenna-Matthews-Olson (FMO) protein. The contribution of the 70-μs component correlates with the amount of FMO protein in the isolated RCC complex. The spectrum of the 1.6-μs component has a sharp bleaching at 835 nm, a maximum at 805 nm, a broad positive band at wavelengths higher than 865 nm, and a broad negative band at wavelengths higher than 960 nm. When the RCC is incubated with inorganic iron and sulfur, the 1.6-μs component is replaced by a component with a lifetime of ∼40 μs, consistent with the reconstruction of the Fx cluster. We propose that the 1.6-μs component results from charge recombination between P840+ and an intermediate electron acceptor operating between Ao and Fx. Our studies in Chlorobium RCCs show that approaches that employ a single wavelength in the measurement of absorption changes have inherent limitations and that a global kinetic analysis at multiple wavelengths in the near-infrared is required to reliably separate absorption changes due to P840/P840+ from the decay of 3Bchl a in the FMO protein.

Original languageEnglish (US)
Pages (from-to)382-393
Number of pages12
JournalBiophysical journal
Volume81
Issue number1
DOIs
StatePublished - Jan 1 2001

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Chlorobium
Chlorobi
Proteins
Sulfur
Genetic Recombination
Iron
Electrons

All Science Journal Classification (ASJC) codes

  • Biophysics

Cite this

Vassiliev, Ilya R. ; Kjær, Bodil ; Schorner, Gregory L. ; Scheller, Henrik V. ; Golbeck, John H. / Photoinduced transient absorbance spectra of P840/P840+ and the FMO protein in reaction centers of Chlorobium vibrioforme. In: Biophysical journal. 2001 ; Vol. 81, No. 1. pp. 382-393.
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Photoinduced transient absorbance spectra of P840/P840+ and the FMO protein in reaction centers of Chlorobium vibrioforme. / Vassiliev, Ilya R.; Kjær, Bodil; Schorner, Gregory L.; Scheller, Henrik V.; Golbeck, John H.

In: Biophysical journal, Vol. 81, No. 1, 01.01.2001, p. 382-393.

Research output: Contribution to journalArticle

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T1 - Photoinduced transient absorbance spectra of P840/P840+ and the FMO protein in reaction centers of Chlorobium vibrioforme

AU - Vassiliev, Ilya R.

AU - Kjær, Bodil

AU - Schorner, Gregory L.

AU - Scheller, Henrik V.

AU - Golbeck, John H.

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N2 - The kinetics of photoinduced absorbance change in the 400-ns to 100-ms time range were studied between 770 and 1025 nm in reaction center core (RCC) complexes isolated from the green sulfur bacterium Chlorobium vibrioforme. A global, multiple stretched-exponential analysis shows the presence of two distinct but strongly overlapping spectra. The spectrum of the 70-μs component consists of a broad bleaching with two minima at 810 and 825 nm and a broad positive band at wavelengths greater than 865 nm and is assigned to the decay of 3Bchl a of the Fenna-Matthews-Olson (FMO) protein. The contribution of the 70-μs component correlates with the amount of FMO protein in the isolated RCC complex. The spectrum of the 1.6-μs component has a sharp bleaching at 835 nm, a maximum at 805 nm, a broad positive band at wavelengths higher than 865 nm, and a broad negative band at wavelengths higher than 960 nm. When the RCC is incubated with inorganic iron and sulfur, the 1.6-μs component is replaced by a component with a lifetime of ∼40 μs, consistent with the reconstruction of the Fx cluster. We propose that the 1.6-μs component results from charge recombination between P840+ and an intermediate electron acceptor operating between Ao and Fx. Our studies in Chlorobium RCCs show that approaches that employ a single wavelength in the measurement of absorption changes have inherent limitations and that a global kinetic analysis at multiple wavelengths in the near-infrared is required to reliably separate absorption changes due to P840/P840+ from the decay of 3Bchl a in the FMO protein.

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