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. Author manuscript; available in PMC: 2009 Aug 26.
Published in final edited form as: Biochemistry. 2008 Aug 2;47(34):9007–9015. doi: 10.1021/bi800419e

Table 2.

Changes in the α-band positions of Co2+Cbl and Co2+Cbi+ caused by the addition of LrPduO in the absence and presence of co-substrate ATP, as determined from the 4.5 K Abs spectra in Figures 2 and 4a

Species Free Corrinoid + LrPduO + LrPduO/ATP
Co2+Cbl 21010 cm−1 (476.0 nm) 21050 cm−1 (475.0 nm) 21480 cm−1 (465.5 nm)
Co2+Cbi+ 21250 cm−1 (470.5 nm) 21250 cm−1 (470.5 nm) 21480 cm−1 (465.5 nm)
a

Note that a blue-shift of the α-band reflects a weakening of the axial ligand–Co2+corrinoid bonding interaction.