Time-dependent XAS studies of trapped enzyme-substrate complexes of alcohol dehydrogenase from Thermoanaerobacter brockii.
The understanding of structure-function relationships in proteins has been significantly advanced with the advent of the biotechnological revolution. A goal yet to be realized for many metalloenzyme systems is to characterize the dynamic changes in structure that bridge the static endpoints provided by crystallography. We present here a series of edge and EXAFS spectra of the metalloenzyme alcohol dehydrogenase from Thermoanaerobacter brockii (TbADH) complexed with its substrate. The enzyme-substrate complexes were trapped by fast freezing at various times, following their enzyme activity. Our edge and EXAFS analyses both reveal the time-dependent changes in the structure of the active site of TbADH.
Kleifeld
O
O
Department of Structural Biology, The Weizmann Institute of Science, Rehovot, Israel.
Frenkel
A
A
Sagi
I
I
D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000378:metabolism; D001421:Bacteria, Anaerobic / Q000201:enzymology*; D000440:Butanols / Q000737:chemistry / Q000378:metabolism; D016988:Gram-Positive Asporogenous Rods, Irregular / Q000201:enzymology*; D009249:NADP / Q000737:chemistry / Q000378:metabolism; D013052:Spectrometry, X-Ray Emission / Q000379:methods
D000440:Butanols; C043958:2-butanol; D009249:NADP; D000426:Alcohol Dehydrogenase