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Title: Electron paramagnetic resonance- (EPR-) resolved kinetics of cryogenic nitric oxide recombination to cytochrome c oxidase and myoglobin

Journal Article · · Biophys. J.; (United States)

By the electron paramagnetic resonance (EPR) technique, recovery kinetics for nitric oxide (NO) to heme following cryogenic photolysis were studied for the nitrosylferrocytochrome a/sub 3/ center in cytochrome c oxidase and for myoglobin. The recovery was nonexponential, as has been observed in previous cryogenic CO and O/sub 2/ rebinding to heme systems. NO rebinding to heme a/sub 3/ started near a temperature of 50 K and was related to a distribution of thermal activation energies. At the peak of the distribution the activation energy was 3.1 kcal/mol, and the preexponential in the recovery rate was 10/sup 9.9/s/sup -1/. For recovery of NO back to the a/sub 3/ heme, the activation energy was threefold less than that for CO where CO binds to nearby Cu/sub a3/ following photolysis from heme a/sub 3/, but was larger than the activation energy for CO, O/sub 2/, and probably NO rebinding to myoglobin. NO ligand rebinding to myoglobin occurred at a temperature as low as 15 K and in a temperature regime where tunneling could occur. However, the rate of NO rebinding to myoglobin did increase with temperature in the 15-25 K range.

Research Organization:
State Univ. of New York, Albany
OSTI ID:
6834934
Journal Information:
Biophys. J.; (United States), Vol. 45:2
Country of Publication:
United States
Language:
English

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