Abstract
Circular dichroic spectra in the visible wavelength region were used to investigate the local environment of Co(II), an activating metal, at the active site of rabbit muscle creatine kinase. There was a small spectral change when CoADP- was bound to creatine kinase, no change when creatine was added, and another small change when NO3- was added to form the transition state analogue. Using matrix rank analysis to quantitate these small spectral changes, a titratable group with a pK = 7.4 was found which modified the enzyme-bound metal-nucleotide interaction. These data suggest that, throughout the enzyme's catalysis, the metal-nucleotide interaction remains very similar in structure to the complex not bound to the enzyme.
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