Key result
In the presence of tetrahydrobiopterin, the rate of NO rebinding to the heme upon photodissociation depends on NO concentration, pointing to a new non-heme NO binding site within eNOS.
Identifies a new tetrahydrobiopterin-dependent non-heme NO binding site in eNOS that may control NO escape.
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Should not change practice; leaves open the functional role of this eNOS site in vivo.
Slama‐Schwok et al. (2002) studied this question. Tetrahydrobiopterin vs. Pterin-depleted eNOS was evaluated on NO rebinding to the heme upon photodissociation. In the presence of tetrahydrobiopterin, the rate of NO rebinding to the heme upon photodissociation depends on NO concentration, pointing to a new non-heme NO binding site within eNOS.
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