The spectral reflectance of petals was measured with a USB2000 spectrophotometer (Ocean Optics, Inc., Ostfildern, Germany) and illumination was provided by a DH-2000-BAL light-source (Ocean Optics, Inc., Ostfildern, Germany), both connected via coaxial fiber cable (QR400–7-UV-VIS, Ocean Optics, Inc., Dunedin, FL, USA). Reflectance was measured relative to a standard white reference tile (Diffuse Reflectance Standard, Spectralon®, labsphere). All reflectance measurements were taken in a constant angle of 90° towards the upper surface of each petal, and the distance between the probe tip and the sample surface was kept constant (5 mm) (cf. Fig. 4a ).
Dh 2000 bal light source
Manufactured by OceanOptics
Sourced in Germany
The DH-2000-BAL is a balanced deuterium-halogen light source designed for a wide range of spectroscopy applications. It provides a stable, uniform output across the ultraviolet (UV) and visible (VIS) spectrum. The light source features two lamp modules, deuterium, and halogen, which can be operated individually or combined to produce a balanced output.
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2 protocols using dh 2000 bal light source
1
Petal Reflectance Spectrophotometry Protocol
2
Monitoring Proton Gradients in Proteoliposomes
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Monitoring ∆ψ in proteoliposomes was carried out at 24°C using a high-resolution CCD array spectrometer (HR2000+, Ocean Optics) combined with a DH-2000-BAL light source (Ocean Optics).
Upon the reaction, optical spectra in the range of 250-680 nm were collected for 600 s. The difference in absorption at 630-590 nm presents ∆ψ-sensitive Oxonol VI response. Optical changes at 340 nm reflect simultaneous NADH consumption. The assay buffer comprised 100 mM 6 MOPS-BTP, 7.0, 1 mM MgSO 4 , 5 mM (NH 4 ) 2 SO 4 , 2.5 µM Oxonol VI, 10 nM solubilized bo 3 oxidase, decylubiquinone (DQ) 100 µM. Prior to measurements proteoliposomes (protein concentration 7-15 µg/ml) were incubated in the assay buffer for 7 min at RT for equilibration of the DQ distribution.
Monitoring ∆pH in proteoliposomes were performed using entrapped pH-sensitive probe trisodium 8-hydroxypyrene-1,3,6-trisulfonate (pyranine) as described in 18 .
Monitoring ∆pH in membrane vesicles was carried out following fluorescence changes of pHsensitive probe acridine orange (AO) with a Hitachi F-7000 fluorescence spectrophotometer, λ ex = 493 nm, λ em = 530 nm at 24°C unless other specified. The assay buffer comprised 50 mM MOPS-BTP, pH 7.2, 100 mM KCl, 1 mM MgCl 2 , 1 µM valinomycin, 100 µM DQ, 1 mM KCN, 3.5 µM AO. The final protein concentration was 150-180 µg/ml.
Upon the reaction, optical spectra in the range of 250-680 nm were collected for 600 s. The difference in absorption at 630-590 nm presents ∆ψ-sensitive Oxonol VI response. Optical changes at 340 nm reflect simultaneous NADH consumption. The assay buffer comprised 100 mM 6 MOPS-BTP, 7.0, 1 mM MgSO 4 , 5 mM (NH 4 ) 2 SO 4 , 2.5 µM Oxonol VI, 10 nM solubilized bo 3 oxidase, decylubiquinone (DQ) 100 µM. Prior to measurements proteoliposomes (protein concentration 7-15 µg/ml) were incubated in the assay buffer for 7 min at RT for equilibration of the DQ distribution.
Monitoring ∆pH in proteoliposomes were performed using entrapped pH-sensitive probe trisodium 8-hydroxypyrene-1,3,6-trisulfonate (pyranine) as described in 18 .
Monitoring ∆pH in membrane vesicles was carried out following fluorescence changes of pHsensitive probe acridine orange (AO) with a Hitachi F-7000 fluorescence spectrophotometer, λ ex = 493 nm, λ em = 530 nm at 24°C unless other specified. The assay buffer comprised 50 mM MOPS-BTP, pH 7.2, 100 mM KCl, 1 mM MgCl 2 , 1 µM valinomycin, 100 µM DQ, 1 mM KCN, 3.5 µM AO. The final protein concentration was 150-180 µg/ml.
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