Effect of temperature on the spectral properties of coenzyme F420 and related compounds.
The uv-visible spectra of 7,8-didemethyl-8-hydroxy-5-deazaflavin-5'-phosphoryllactyl glutamate (coenzyme F420), a naturally occurring 5-deazaflavin derivative, in three different buffers changed with a rise in temperature; the effect on the extinction coefficient at 420 nm (epsilon 420) was as follows: In phosphate-buffered solutions at pH less than 7.5, the epsilon 420 increased (at pH 5.0 for a temperature shift from 15 to 60 degrees C, delta epsilon 420 was +87%), but between pH 7.5 and 8, epsilon 420 changed very little. At pH greater than 8.0 in phosphate- or borate-buffered solutions, epsilon 420 decreased slightly. In morpholineethanesulfonic acid (Mes)-buffered F420 solutions at pH 5 and 5.5, epsilon 420 changed very little, whereas at pH 6-8, the epsilon 420 decreased. Absorbance of F420 at 401 nm in phosphate buffer at pH 5 to 9 was not significantly affected by temperature. Changes in epsilon 420 due to temperature change corresponded to changes in the pKa of 8-OH of the deazaflavin molecule; studies with adenylated F420 showed that the 8-OH of F420 was responsible for these changes.(ABSTRACT TRUNCATED AT 250 WORDS)
Purwantini
E
E
Department of Microbiology, University of Iowa, Iowa City 52242.
Mukhopadhyay
B
B
Spencer
R W
RW
Daniels
L
L
D000465:Algorithms; D002021:Buffers; D006863:Hydrogen-Ion Concentration; D012256:Riboflavin / Q000031:analogs & derivatives* / Q000737:chemistry; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
D002021:Buffers; C015084:coenzyme F420; D012256:Riboflavin