. Author manuscript; available in PMC: 2012 May 17.

Published in final edited form as: Biochemistry. 2011 Apr 22;50(19):3879–3890. doi: 10.1021/bi101702c

Table 2.

Spectral and enzymatic properties of CcO purified from R. sphaeroides wild-type (2.4.1+CcO) and cardiolipin-depleted (CL3+CcO) cell lines

Cell Line	Genotype	Spectral Peaks of Purified CcO (nm)		Activity (s⁻¹) no added lipid	Activity (s⁻¹) plus added lipid	Increase in activity with lipid
Cell Line	Genotype	Soret	Alpha	Activity (s⁻¹) no added lipid	Activity (s⁻¹) plus added lipid	Increase in activity with lipid
2.4.1+CcO	wild-type	445	606	1050 ± 100^#	1340 ± 50^#	28 ± 2%^#
CL3 +CcO	Δcls	445	606	1060 ± 109^@	1410 ± 120^@	33 ± 8%^@

Keys: Both strains produced his-tagged CcO from a plasmid (PRK-pYJ123H (36)). The Soret and alpha peaks were from the optical spectra of dithionite-reduced CcO. The molecular activity of purified CcO was measured at pH 6.5 and presented as turnover number (moles cytochrome c oxidized per mole CcO per second). The number of independent measurements was 3^# or 5^@.