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. 1999 Aug 17;96(17):9591–9596. doi: 10.1073/pnas.96.17.9591

Table 1.

Selected resonance Raman frequencies (Ex. 413.1 nm) of various preparations of A. ambivalens aa3 quinol oxidase in the reduced state

Enzyme ν4 ν11(a) ν2 (a) νC=O (formyl, a3)
Purified, t = 1 min* 1,355 1,520 1,587 1,660
Purified, t ∼ 30 min 1,355 1,520 1,587 1,667
Purified + UQ, t ∼ 10 min 1,355 1,520 1,587 1,667
Intact membrane 1,355 1,519 1,587 1,667
Membrane extract 1,356 1,519 1,588 1,667.5
Bovine§ 1,354 1,517 1,586 1,664

The enzyme samples were reduced by addition of a degassed dithionite solution under anaerobic conditions. 

*

Purified aa3in 100 mM phosphate buffer, pH 7.4, 0.3 mg/ml lauryl maltoside, spectrum recorded ∼1 min after reduction by dithionite. 

The purified oxidized aa3 was preincubated with 1.6 mg/ml decylubiquinone (UQ) for 1 hr and then was reduced by dithionite. Spectrum was recorded after 10 min. 

Membranes dissolved in lauryl maltoside (2g LM/1 g protein). 

§

Data from Argade et al. (30) on bovine cytochrome c oxidase.