Title : Sensitivity of flavin fluorescence dynamics in neuronal nitric oxide synthase to cofactor-induced conformational changes and dimerization.

Pub. Date : 1998 Dec 15

PMID : 9860870






5 Functional Relationships(s)
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1 Sensitivity of flavin fluorescence dynamics in neuronal nitric oxide synthase to cofactor-induced conformational changes and dimerization. 4,6-dinitro-o-cresol nitric oxide synthase 1 Homo sapiens
2 The fluorescence intensity of the two flavin prosthetic groups, FMN and FAD, in neuronal nitric oxide synthase (nNOS) was found to decay highly nonexponentially, being best described by four fluorescence lifetimes. 4,6-dinitro-o-cresol nitric oxide synthase 1 Homo sapiens
3 The fluorescence intensity of the two flavin prosthetic groups, FMN and FAD, in neuronal nitric oxide synthase (nNOS) was found to decay highly nonexponentially, being best described by four fluorescence lifetimes. 4,6-dinitro-o-cresol nitric oxide synthase 1 Homo sapiens
4 Investigating nNOS in the absence of one or more of Ca2+/calmodulin, tetrahydrobiopterin, and heme revealed an influence of these cofactors on the microenvironments of the flavin prosthetic groups. 4,6-dinitro-o-cresol nitric oxide synthase 1 Homo sapiens
5 Similar effects on the flavin rotational dynamics were found by analyzing the fluorescence anisotropy decay of the holo and of the different apo forms of nNOS. 4,6-dinitro-o-cresol nitric oxide synthase 1 Homo sapiens