Summary
Methods for the study of rapid reactions region at cryogenic temperatures are reviewed from the standpoint of range of kinetic constants, signal-to-noise ratio and compatability of optical methods with X-ray absorption spectroscopy. Alternation of optical monitoring with X-ray absorption spectroscopy and optical pumping of the sample are treated, and appropriate apparatus designs are reviewed. Typical results of structural studies at 4 and 40 K are described and the accumulation of the ligand at about 3Â from the iron atom in a protein structural crevice or “energy minimum” is described. The generality of the idea of metal atom substrate binding sites, supplemented with adjacent protein binding sites, which act to “dock” the ligand and allow transfer to the active site with appropriate orientation and collision frequency, is suggested. The possibility that the “docking site” mechanism extends to other proteins and enzymes is suggested.
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Chance, B., Powers, L., Chance, M., Zhou, Y., Reddy, K.S. (1987). Optical and X-Ray Techniques in the Study of Rapid Ligand Binding: A Ligand „Docking“ Site in the Reaction of Mb and Co At 40 K. In: Kim, C.H., Tedeschi, H., Diwan, J.J., Salerno, J.C. (eds) Advances in Membrane Biochemistry and Bioenergetics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8640-7_40
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